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Pattern recognition receptor
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Pattern recognition receptors (PRRs)[1] play a crucial role in the proper function of the innate immune system. PRRs are germline-encoded host sensors, which detect molecules typical for the pathogens[2]. They are proteins expressed, mainly, by cells of the innate immune system, such as dendritic cells, macrophages, monocytes, neutrophils and epithelial cells[3][4], to identify two classes of molecules: pathogen-associated molecular patterns (PAMPs), which are associated with microbial pathogens, and damage-associated molecular patterns (DAMPs), which are associated with components of host's cells that are released during cell damage or death. They are also called primitive pattern recognition receptors because they evolved before other parts of the immune system, particularly before adaptive immunity. PRRs also mediate the initiation of antigen-specific adaptive immune response and release of inflammatory cytokines[2][5]
Contents
[hide]
1 Molecules recognized
2 Classification
3 PRR types and localization
3.1 Membrane-bound PRRs
3.1.1 Receptor kinases
3.1.2 Toll-like receptors (TLR)
3.1.2.1 The TLR signaling
3.1.3 C-type lectin receptors (CLR)
3.1.3.1 CLR signaling
3.1.3.2 Group I CLRs: The mannose receptors[22]
3.1.3.3 Group II CLRs: asialoglycoprotein receptor family
3.2 Cytoplasmic PRRs
3.2.1 NOD-like receptors (NLR)
3.2.1.1 NLR signaling
3.2.1.2 NODs
3.2.1.3 NLRPs
3.2.1.4 Other NLRs
3.2.2 RIG-I-like receptors (RLR)
3.2.2.1 RLR signaling
4 Plant PRRs
4.1 NonRD kinases
4.2 Secreted PRRs
5 PRRs in human medicine
6 References
7 External links
Molecules recognized[edit]
The microbe-specific molecules that are recognized by a given PRR are called pathogen-associated molecular patterns (PAMPs) and include bacterial carbohydrates (such as lipopolysaccharide or LPS, mannose), nucleic acids (such as bacterial or viral DNA or RNA), bacterial peptides (flagellin, microtubule elongation factors), peptidoglycans and lipoteichoic acids (from Gram-positive bacteria), N-formylmethionine, lipoproteins and fungal glucans and chitin.
Endogenous stress signals are called damage-associated molecular patterns (DAMPs) and include uric acid and extracellular ATP, among many other compounds[2].
Classification[edit]
There are several subgroups of PRRs. They are classified according to their ligand specificity, function, localization and/or evolutionary relationships. Based on their localization, PRRs may be divided into membrane-bound PRRs and cytoplasmic PRRs.
Membrane-bound PRRs include Toll like receptors (TLRs) and C-type lectin receptors (CLRs).
Cytoplasmic PRRs include NOD-like receptors (NLRs) and RIG-I-like receptors (RLRs).
PRR types and localization[edit]
Membrane-bound PRRs[edit]
Receptor kinases[edit]
PRRs were first discovered in plants.[6] Since that time many plant PRRs have been predicted by genomic analysis (370 in rice; 47 in Arabidopsis). Unlike animal PRRs, which associated with intracellular kinases via adaptor proteins (see non-RD kinases below), plant PRRs are composed of an extracellular domain, transmembrane domain, juxtamembrane domain and intracellular kinase domain as part of a single protein.
Toll-like receptors (TLR)[edit]
Recognition of extracellular or endosomal pathogen-associated molecular patterns is mediated by transmembrane proteins known as toll-like receptors (TLRs).[7] TLRs share a typical structural motif, the Leucine rich repeats (LRR), which give them their specific appearance and are also responsible for TLR functionality[8]. Toll-like receptors were first discovered in Drosophila and trigger the synthesis and secretion of cytokines and activation of other host defense programs that are necessary for both innate or adaptive immune responses. 10 functional members of the TLR family have been described in humans so far[9]. Studies have been conducted on TLR11 as well, and it has been shown that it recognizes flagellin and profilin-like proteins in mice[10]. Nonetheless, TLR11 is only a pseudogene in humans without direct function or functional protein expression. Each of the TLR has been shown to interact with a specific PAMP[5][11][12].
The TLR signaling[edit]
TLRs tend to dimerize, TLR4 forms homodimers, and TLR6 can dimerize with either TLR1 or TLR2. [11] Interaction of TLRs with their specific PAMP is mediated through either MyD88- dependent pathway and triggers the signaling through NF-κB and the MAP kinase pathway and therefore the secretion of pro-inflammatory cytokines and co-stimulatory molecules or TRIF - dependent signaling pathway[2][5][11]. MyD88 - dependent pathway is induced by various PAMPs stimulating the TLRs on macrophages and dendritic cells. MyD88 attracts the IRAK4 molecule, IRAK4 recruits IRAK1 and IRAK2 to form a signaling complex. The signaling complex reacts with TRAF6 which leads to TAK1 activation and consequently the induction of inflammatory cytokines.The TRIF-dependent pathway is induced by macrophages and DCs after TLR3 and TLR4 stimulation.[2] Molecules released following TLR activation signal to other cells of the immune system making TLRs key elements of innate immunity and adaptive immunity.[2][13][14]
C-type lectin receptors (CLR)[edit]
Many different cells of the innate immune system express a myriad of CLRs which shape innate immunity by virtue of their pattern recognition ability.[15] Even though, most classes of human pathogens are covered by CLRs, CLRs are a major receptor for recognition of funghi[16][17]: nonetheless, other PAMPs have been identifies in studies as targets of CLRs as well e.g. mannose is the recognition motif for many viruses, fungi and mycobacteria; similarly fucose presents the same for certain bacteria and helminths; and glucans are present on mycobacteria and fungi. In addition, many of acquired nonself surfaces e.g. carcinoembryonic/oncofetal type neoantigens carrying "internal danger source"/"self turned nonself" type pathogen pattern are also identified and destroyed (e.g. by complement fixation or other cytotoxic attacks) or sequestered (phagocytosed or ensheathed) by the immune system by virtue of the CLRs. The name lectin is a bit misleading because the family includes proteins with at least one C-type lectin domain (CTLD) which is a specific type of carbohydrate recognition domain. CTLD is a ligand binding motif found in more than 1000 known proteins (more than 100 in humans) and the ligands are often not sugars.[18] If and when the ligand is sugar they need Ca2+ – hence the name "C-type", but many of them don't even have a known sugar ligand thus despite carrying a lectin type fold structure, some of them are technically not "lectin" in function.
CLR signaling[edit]
There are several types of signaling involved in CLRs induced immune response, major connection has been identified between TLR and CLR signaling, therefore we differentiate between TLR-dependent and TLR-independent signaling. DC-SIGN leading to RAF1-MEK-ERK cascade, BDCA2 signaling via ITAM and signaling through ITIM belong among the TLR-dependent signaling. TLR-independent signaling such as Dectin 1, and Dectin 2 - mincle signaling lead to MAP kinase and NFkB activation[19][20].
Membrane receptor CLRs have been divided into 17 groups based on structure and phylogenetic origin.[21] Generally there is a large group, which recognizes and binds carbohydrates, so called carbohydrate recognition domains (CRDs) and the previously mentioned CTLDs.
Another potential characterization of the CLRs can be into mannose receptors and asialoglycoprotein receptors[19].
Group I CLRs: The mannose receptors[22][edit]
The mannose receptor (MR) is a PRR primarily present on the surface of macrophages and dendritic cells. It belongs into the calcium-dependent multiple CRD group.[16] The MR belongs to the multilectin receptor protein group and, like the TLRs, provides a link between innate and adaptive immunity.[23][24] It recognizes and binds to repeated mannose units on the surfaces of infectious agents and its activation triggers endocytosis and phagocytosis of the microbe via the complement system. Specifically, mannose binding triggers recruitment of MBL-associated serine proteases (MASPs). The serine proteases activate themselves in a cascade, amplifying the immune response: MBL interacts with C4, binding the C4b subunit and releasing C4a into the bloodstream; similarly, binding of C2 causes release of C2b. Together, MBL, C4b and C2a are known as the C3 convertase. C3 is cleaved into its a and b subunits, and C3b binds the convertase. These together are called the C5 convertase. Similarly again, C5b is bound and C5a is released. C5b recruits C6, C7, C8 and multiple C9s. C5, C6, C7, C8 and C9 form the membrane attack complex (MAC).
Group II CLRs: asialoglycoprotein receptor family[edit]
This is another large superfamily of CLRs that includes
The classic asialoglycoprotein receptor macrophage galactose-type lectin (MGL)
DC-SIGN (CLEC4L)
Langerin (CLEC4K)
Myeloid DAP12‑associating lectin (MDL)‑1 (CLEC5A)
DC‑associated C‑type lectin 1 (Dectin1) subfamily which includes
dectin 1/CLEC7A
DNGR1/CLEC9A
Myeloid C‑type lectin‑like receptor (MICL) (CLEC12A)
CLEC2 (also called CLEC1B)- the platelet activation receptor for podoplanin on lymphatic endothelial cells and invading front of some carcinomas.
CLEC12B
DC immunoreceptor (DCIR) subfamily which includes:
DCIR/CLEC4A
Dectin 2/CLEC6A
Blood DC antigen 2 (BDCA2) ( CLEC4C)
Mincle i.e. macrophage‑inducible C‑type lectin (CLEC4E)
The nomenclature (mannose versus asialoglycoprotein) is a bit misleading as these the asialoglycoprotein receptors are not necessarily galactose (one of the commonest outer residues of asialo-glycoprotein) specific receptors and even many of this family members can also bind to mannose after which the other group is named.
Cytoplasmic PRRs[edit]
NOD-like receptors (NLR)[edit]
For more details, see NOD-like receptor.
The NOD-like receptors (NLRs) are cytoplasmic proteins, which recognize bacterial peptidoglycans and mount proinflammatory and antimicrobial immune response[25]. Approximately 20 of these proteins have been found in the mammalian genome and include nucleotide-binding oligomerization domain (NODs), which binds nucleoside triphosphate. Among other proteins the most important are: the MHC Class II transactivator (CIITA), IPAF, BIRC1 etc.[26]
NLR signaling[edit]
Some of these proteins recognize endogenous or microbial molecules or stress responses and form oligomers that, in animals, activate inflammatory caspases (e.g. caspase 1) causing cleavage and activation of important inflammatory cytokines such as IL-1, and/or activate the NF-κB signaling pathway to induce production of inflammatory molecules.
The NLR family is known under several different names, including the CATERPILLER (or CLR) or NOD-LRR family.[26][27] The most significant members of the NLRs are NOD1 and NOD2. They sense the conserved microbial peptidoglycans in the cytoplasm of the cell and therefore represent another level of immune response after membrane-bound receptors such as TLRs and CLRs.[25] This family of proteins is greatly expanded in plants, and constitutes a core component of plant immune systems.[28]
NODs[edit]
The ligands are currently known for NOD1 and NOD2. NOD1 recognizes a molecule called meso-DAP, which is a peptidoglycan constituent only of Gram negative bacteria. NOD2 proteins recognize intracellular MDP (muramyl dipeptide), which is a peptidoglycan constituent of both Gram positive and Gram negative bacteria. When inactive, NODs are in the cytosol in a monomeric state and they undergo conformational change only after ligand recognition, which leads to their activation.[25] NODs transduce signals in the pathway of NF-κB and MAP kinases via the serine-threonine kinase called RIP2. NODs signal via N-terminal CARD domains to activate downstream gene induction events, and interact with microbial molecules by means of a C-terminal leucine-rich repeat (LRR) region.[29]
The interaction and cooperation among different types of receptors typical for the innate immune system has been established. An interesting cooperation has been discovered between TLRs and NLRs, particularly between TLR4 and NOD1 in response to Escherichia coli infection.[30] Another proof of the cooperation and integration of the entire immune system has been shown in vivo, when TLR signaling was inhibited or disabled, NOD receptors took over role of TLRs.[31]
NLRPs[edit]
Like NODs, these proteins contain C-terminal LRRs, which appear to act as a regulatory domain and may be involved in the recognition of microbial pathogens. Also like NODs, these proteins contain a nucleotide binding site (NBS) for nucleoside triphosphates. Interaction with other proteins (e.g. the adaptor molecule ASC) is mediated via N-terminal pyrin (PYD) domain. There are 14 members of this protein subfamily in humans (called NLRP1 to NLRP14). NLRP3 and NLRP4 are responsible for the inflammasome activation.[32] NLRP3 can be activated and give rise to NLRP3 inflammasome by ATP, bacterial pore-forming toxins, alum and crystals. Alongside the listed molecules, which lead to activation of NLRP3 inflammasome, the assembly and activation can also be induced by K+ efflux, Ca2+ influx, disruption of lysosomes and ROS originating from mitochondria.[33] The NLRP3 inflammasome is essential for induction of effective immune response. The NLRP3 inflammasome can be induced by a wide range of stimuli in contrast to the NLRP4 inflammasome, which binds more limited number and variety of ligands and works in a complex with NAIP protein.[34]
Other NLRs[edit]
Other NLRs such as IPAF and NAIP5/Birc1e have also been shown to activate caspase-1 in response to Salmonella and Legionella.
RIG-I-like receptors (RLR)[edit]
Further information: RIG-I-like receptor
Three RLR helicases have so far been described: RIG-I and MDA5 (recognizing 5'triphosphate-RNA and dsRNA, respectively), which activate antiviral signaling, and LGP2, which appears to act as a dominant-negative inhibitor. RLRs initiate the release of inflammatory cytokines and type I interferon (IFN I)[2].
RLR signaling[edit]
RLRs, are RNA helicases, which have been shown to participate in intracellular recognition of viral double-stranded (ds) and single stranded RNA which recruit factors via twin N-terminal CARD domains to activate antiviral gene programs, which may be exploited in therapy of viral infections.[35][36] It has been suggested that the main antiviral program induced by RLR is based on ATPase activity[37]. RLRs often interact and create cross-talk with the TLRs in the innate immune response and in regulation of adaptive immune response.[38]
RIG-I and Mda5-mediated signalling pathway.
Plant PRRs[edit]
Plants contain a significant number of PRRs that share remarkable structural and functional similarity with drosophila TOLL and mammalian TLRs. The first PRR identified in plants or animals was the Xa21 protein, conferring resistance to the Gram-negative bacterial pathogen Xanthomonas oryzae pv. oryzae.[6][39] Since that time two other plants PRRs, Arabidopsis FLS2 (flagellin) and EFR (elongation factor Tu receptor)have been isolated.[40] The corresponding PAMPs for FLS2 and EFR have been identified.[40] Upon ligand recognition, the plant PRRs transduce "PAMP-triggered immunity" (PTI).[41] Plant immune systems also encode resistance proteins that resemble NOD-like receptors (see above), that feature NBS and LRR domains and can also carry other conserved interaction domains such as the TIR cytoplasmic domain found in Toll and Interleukin Receptors.[42] The NBS-LRR proteins are required for effector triggered immunity (ETI).
NonRD kinases[edit]
PRRs commonly associate with or contain members of a monophyletic group of kinases called the interleukin-1 receptor-associated kinase (IRAK) family that include Drosophila Pelle, human IRAKs, rice XA21 and Arabidopsis FLS2. In mammals, PRRs can also associate with members of the receptor-interacting protein (RIP) kinase family, distant relatives to the IRAK family. Some IRAK and RIP family kinases fall into a small functional class of kinases termed non-RD, many of which do not autophosphorylate the activation loop. A survey of the yeast, fly, worm, human, Arabidopsis, and rice kinomes (3,723 kinases) revealed that despite the small number of non-RD kinases in these genomes (9%–29%), 12 of 15 kinases known or predicted to function in PRR signaling fall into the non-RD class. In plants, all PRRs characterized to date belong to the non-RD class. These data indicate that kinases associated with PRRs can largely be predicted by the lack of a single conserved residue and reveal new potential plant PRR subfamilies.[43][44]
Secreted PRRs[edit]
A number of PRRs do not remain associated with the cell that produces them. Complement receptors, collectins, ficolins, pentraxins such as serum amyloid and C-reactive protein, lipid transferases, peptidoglycan recognition proteins (PGRs) and the LRR, XA21D[45] are all secreted proteins. One very important collectin is mannan-binding lectin (MBL), a major PRR of the innate immune system that binds to a wide range of bacteria, viruses, fungi and protozoa. MBL predominantly recognizes certain sugar groups on the surface of microorganisms but also binds phospholipids, nucleic acids and non-glycosylated proteins.[46] Once bound to the ligands MBL and Ficolin oligomers recruit MASP1 and MASP2 and initiate the lectin pathway of complement activation which is somewhat similar to the classical complement pathway.
PRRs in human medicine[edit]
Research groups have recently conducted extensive research into the involvement and potential use of patient's immune system in the therapy of various diseases, the so called immunotherapy, including monoclonal antibodies, non-specific immunotherapies, oncolytic virus therapy, T-cell therapy and cancer vaccines.[47] NOD2 has been associated through a loss- and gain- of function with development of Crohn's disease and early-onset sarcoidosis[25][48]. Mutations in NOD2 in cooperation with environmental factors lead to development of chronic inflammation in the intestine. [25][49] Therefore, it has been suggested to treat the disease by inhibiting the small molecules, which are able to modulate the NOD2 signaling, particularly RIP2. Two therapeutics have been approved by FDA so far inhibiting the phosphorylation on RIP2, which is necessary for proper NOD2 functioning, gefitinib and erlotinib. [50][51] Additionally, research has been conducted on GSK583, a highly specific RIP2 inhibitor, which seems highly promising in inhibiting NOD1 and NOD2 signaling and therefore, limiting inflammation caused by NOD1, NOD2 signaling pathways.[52] Another possibility is to remove the sensor for NOD2, which has been proved efficient in murine models in the effort to suppress the symptoms of Crohn's disease.[53] Type II kinase inhibitors, which are highly specific, have shown promising results in blocking the TNF arising from NOD-dependent pathways, which is shows a high potential in treatment of inflammation associated tumors.[54]
Another possible exploitation of PRRs in human medicine is also related to tumor malignancies of the intestines. Helicobacter pylori has been shown by studies to significantly correlate with the development of a gastrointestinal tumors. In a healthy individual Helicobacter pylori infection is targeted by the combination of PRRs, namely TLRs, NLRs, RLRs and CLR DC-SIGN. In case of their malfunction, these receptors have also been connected to carcinogenesis. When the Helicobacter pylori infection is left to progress in the intestine it develops into chronic inflammation, atrophy and eventually dysplasia leading to development of cancer. Since all types of PRRs play a role in the identification and eradication of the infection, their specific agonists mount a strong immune response to cancers and other PRR-related diseases. The inhibition of TLR2 has been shown to significantly correlate with improved state of the patient and suppression of the gastric adenocarcinoma.[55]
The PRRs are also tightly connected to the proper function of neuronal networks and tissues, especially because of their involvement in the processes of inflammation, which are essential for proper function but may cause irreparable damage if not under control. The TLRs are expressed on most cells of the central nervous system (CNS) and they play a crucial role in sterile inflammation. After an injury, they lead to impairment of axonal growth and slow down or even halt the recovery altogether. Another important structure involved in and potentially exploitable in therapy after injury is the inflammasome. Through its induction of proinflammatory cytokines, IL-1β and IL-18 it has been proposed, that inhibition of inflammasome may also serve as an efficient therapeutic method.[56] The involvement of inflammasome has also been researched in several other diseases including experimental autoimmune encephalomyelitis (EAE), Alzheimer's and Parkinson's diseases and in atherosclerosis connected with type II diabetes in patients. The suggested therapies include degradation of NLRP3 or inhibit the proinflammatory cytokines.[57]
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Jump up ^ Tigno-Aranjuez, Justine T.; Benderitter, Pascal; Rombouts, Frederik; Deroose, Frederik; Bai, XiaoDong; Mattioli, Benedetta; Cominelli, Fabio; Pizarro, Theresa T.; Hoflack, Jan (2014-10-24). "In Vivo Inhibition of RIPK2 Kinase Alleviates Inflammatory Disease". Journal of Biological Chemistry. 289 (43): 29651–29664. doi:10.1074/jbc.m114.591388. ISSN 0021-9258. PMID 25213858.
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External links[edit]
Pattern Recognition Receptors at the US National Library of Medicine Medical Subject Headings (MeSH)
[hide]
v
t
e
Innate immune system: Pattern recognition receptors
Membrane-bound_PRRs
Toll-like receptor
Mannose receptor
Formyl peptide receptor
Scavenger receptor
Cytoplasmic_PRRs
Toll-like receptor
NOD-like receptor
RIG-I-like receptor
Scavenger receptor
Secreted_PRRs
Complement receptor
Collectin
Other/ungrouped
Immunophilins (Cyclophilin)
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text:
Prime Minister of Brazil
From Wikipedia, the free encyclopedia
Jump to: navigation, search
The political position of Prime Minister of Brazil existed in two different parliamentary periods in the country's history: from 1847 to 1889 (during most of the Empire) and from 1961 to 1963 (during the last years of the Second Republic).
The official title of the Prime Minister was President of the Council of Ministers in both periods, and he was referred to by the press and the people as President of the Cabinet in the imperial era or Premier in the republican era.
Below are more detailed descriptions of the post in each period.
Contents
[hide]
1 President of the Council of Ministers of the Empire of Brazil (1847–1889)
1.1 List of Presidents of the Council of Ministers of the Empire of Brazil
1.1.1 The proclamation of the Republic as a coup to force the removal of the Prime Minister
2 President of the Council of Ministers of the United States of Brazil (1961–1963)
2.1 List of Presidents of the Council of Ministers of the United States of Brazil
3 Timeline
4 See also
5 References
President of the Council of Ministers of the Empire of Brazil (1847–1889)[edit]
Prime Minister of the Empire of Brazil
Grand imperial coat of arms
The Viscount of Rio Branco, the most successful and longest serving officeholder
Residence
Rio de Janeiro, Empire of Brazil
Appointer
Emperor of Brazil (1847–1889)
Formation
22 August 1847
First holder
The 2nd Viscount of Caravelas
Final holder
The Viscount of Ouro Preto
Abolished
15 November 1889
The political position of Prime Minister of Brazil was first being created in 1847 by the Brazilian Emperor Pedro II officially as President of the Council of Ministers, but he was referred to by the press and the people as President of the Cabinet. Often, the title President of the Council, a shortened version of the official style, was also employed.
The written Constitution of the Brazilian Empire did not require the Emperor to appoint a prime minister; nor did it provide for a parliamentary system of government, instead vesting the Executive authority in the Emperor himself, and stipulating that the Emperor was to be aided by ministers that he was free to appoint and dismiss. However, Emperor Pedro II decided to appoint a president of the Council among his ministers, to lead the workings of the Government. He also chose to create a sort of parliamentary government, whereby the prime minister would be someone who could command a majority in the Chamber of Deputies, the lower House of the Brazilian Imperial Parliament, known as General Assembly. Therefore, even without being required by the Constitution, the Emperor started to exercise his authority in a manner compatible with parliamentary government, only appointing as prime minister someone who could retain parliamentary support, etc.
However, the emperor didn't become a figurehead monarch like other heads of State in a parliamentary system. The prime minister needed to retain the political confidence both of a majority of the Chamber of Deputies and of the Emperor, who actively scrutinized the workings of the Government. Sometimes the Emperor would dissolve the Chamber of Deputies and summon new elections (a power he possessed under the Constitution), or dismiss the prime minister, due to his own political beliefs about the efficiency of the Government. Thus, the Emperor would often dismiss a prime minister, and then appoint someone else from the same party. All this led to a succession of short-lived Cabinets. The emperor retained decision-making powers with regard to the signature or veto of bills passed by Parliament, and would not always abide by the advice of his ministers. And that was seen as normal given that the monarch wasn't required by the Constitution to reign in a parliamentary system, and the establishment of one was only a limited and voluntary decision of Pedro II.
Therefore, the parliamentary system voluntarily established by Emperor Pedro II wasn't identical to the standard of a parliamentary government with a Head of State that reigns but does not govern, given that the Emperor retained part of the control over the daily affairs of his government. Thus, the parliamentary system that was put in place in the reign of Pedro II can be termed a semi-parliamentary Government, and can be compared to the political system of some republics, such as France, that are governed under a semi-presidential system, in which the Head of State has more than just the customary reserve powers, but there is also a prime minister who needs to maintain the confidence of Parliament in order to retain his office.
This co-existence of a Head of State with real powers and influence with a prime minister responsible before Parliament was dubbed by many Brazilian political scientists as parlamentarismo às avessas (backwards parliamentarism), a criticism corresponding to their view that, in the parliamentary system created by Emperor Pedro II, the Chamber of Deputies was the weaker party, and the survival of the Cabinet depended more on the confidence of the Emperor than in that of Parliament.
Shortcomings in party loyalty, with members of Parliament and groups of members rooting for their own interests and not always abiding by the directives of the party leadership also contributed greatly to short-lived Cabinets. Indeed, it was very common for a Prime Minister to be replaced due to lack of support from his party's backbenchers, causing the Prime Minister to be replaced with somebody else from the same party, during the same Parliament.
During the forty-nine years of Pedro II's personal reign, from 1840 until 1889 there were sixteen parliamentary elections (eleven provoked by the dissolution of Parliament by the Emperor at the Prime Minister's request, with the summoning of new elections, and five others provoked by the expiration of the term of office of the members of the Chamber of Deputies). This means that, on average, each legislature of the Chamber of Deputies had a life span slightly superior to three years. However, in the forty two years between the creation of the office of Prime Minister in 1847 and its abolition in 1889, there were thirty two appointments to the presidency of the Council, which means that prime ministerships lasted on average a little more than a year and four months. Certain politicians, however, like the Duke of Caxias, Marquis of Olinda, and Zacarias Góis e Vasconcellos managed to regain the prime ministership after having lost it. Caxias and Zacarias Góis e Vasconcellos each served three times as President of the Council, while Olinda held the office of Prime Minister for a record of four times.
The president of the Council owed his position to both his party's majority in the Legislature (and to his party's willingness to support him in the Chamber) and to the Emperor, and these two sources of authority (parliamentary backing and imperial appointment) could sometimes come into conflict. 19th century abolitionist leader and historian Joaquim Nabuco said:
The President of the Council in Brazil was no Russian Chancellor, Sovereign's creature, nor a British Prime Minister, made only by the trust of the Commons: the delegation of the Crown was to him as necessary and important as the delegation of the Chamber, and, to exert with safety his functions, he had to dominate the caprice, the oscillations and ambitions of the Parliament, as well as to preserve always unalterable the favor, the good will of the Emperor.[1]"
— Joaquim Nabuco, 1899
The shortest prime-ministership was the first of the three periods of Zacarias Góis e Vasconcellos in office, when he occupied the presidency of the Council for just a few days in May 1862 before being replaced. The longest continuous prime-ministership corresponded to the period when the Viscount of Rio Branco was in office: he served as President of the Council from March 1871 until June 1875. The Viscount of Rio Branco served as Prime Minister only once, however, and his period of service as Prime Minister is surpassed by the total duration of the four non-consecutive premierships of the Marquis of Olinda, making Olinda the longest serving President of the Council if non-consecutive time is considered.
The position of prime minister was abolished with the deposition of the Monarchy in 1889.
List of Presidents of the Council of Ministers of the Empire of Brazil[edit]
Parties
Conservative Party
Liberal Party
Progressive League
#
Name
Portrait
Took Office
Left Office
Party
1 Manuel Alves Branco
2nd Viscount of Caravelas 22 August 1847 8 March 1848 Liberal Party
2 José Carlos Pereira de Almeida Torres
Viscount of Macaé 8 March 1848 31 March 1848 Liberal Party
3 Francisco de Paula Sousa e Melo 31 March 1848 29 September 1848 Liberal Party
4 Pedro de Araújo Lima
Viscount, later Marquis of Olinda 29 September 1848 8 October 1849 Conservative Party
5 José da Costa Carvalho
Marquis of Monte Alegre 8 October 1849 11 May 1852 Conservative Party
6 Joaquim Rodrigues Torres
Viscount of Itaborai 11 May 1852 6 September 1853 Conservative Party
7 Honório Hermeto Carneiro Leão
Marquis of Paraná 6 September 1853 3 September 1856 Conservative Party
8 Luís Alves de Lima e Silva
Duke of Caxias (then Marquis) 3 September 1856 4 May 1857 Conservative Party
9 Pedro de Araújo Lima
Marquis of Olinda 4 May 1857 12 December 1858 Conservative Party
10 Viscount of Abaeté 12 December 1858 10 August 1859 Conservative Party
11 Baron of Uruguaiana 10 August 1859 2 March 1861 Conservative Party
12 Duke of Caxias (then Marquis) 2 March 1861 24 May 1862 Conservative Party
13 Zacarias de Góis e Vasconcelos 24 May 1862 30 May 1862 Progressive League
14 Marquis of Olinda 30 May 1862 15 January 1864 Progressive League
15 Zacarias de Góis e Vasconcelos 15 January 1864 31 August 1864 Progressive League
16 Francisco José Furtado 31 August 1864 12 May 1865 Liberal Party
17 Marquis of Olinda 12 May 1865 3 August 1866 Liberal Party
18 Zacarias de Góis e Vasconcelos 3 August 1866 16 July 1868 Liberal Party
19 Viscount of Itaboraí 16 July 1868 29 September 1870 Conservative Party
20 Viscount, later Marquis of São Vicente 29 September 1870 7 March 1871 Conservative Party
21 Viscount of Rio Branco 7 March 1871 25 June 1875 Conservative Party
22 Duke of Caxias 25 June 1875 5 January 1878 Conservative Party
23 Viscount of Sinimbu 5 January 1878 28 March 1880 Liberal Party
24 José Antônio Saraiva 28 March 1880 21 January 1882 Liberal Party
25 Martinho Álvares da Silva Campos 21 January 1882 3 July 1882 Liberal Party
26 Viscount, later Marquis of Paranaguá 3 July 1882 24 May 1883 Liberal Party
27 Lafayette Rodrigues Pereira 24 May 1883 6 June 1884 Liberal Party
28 Manuel Pinto de Sousa Dantas 6 June 1884 6 May 1885 Liberal Party
29 José Antônio Saraiva 6 May 1885 20 August 1885 Liberal Party
30 Baron of Cotegipe 20 August 1885 10 March 1888 Conservative Party
31 João Alfredo Correia de Oliveira 10 March 1888 7 June 1889 Conservative Party
32 Viscount of Ouro Preto 7 June 1889 15 November 1889 Liberal Party
The proclamation of the Republic as a coup to force the removal of the Prime Minister[edit]
The events of the Brazilian Proclamation of the Republic on November 15, 1889 started as an unprecedented military coup to remove the Prime Minister, who had been appointed by the Emperor and who enjoyed the confidence of the Chamber of Deputies, the lower house of the General Assembly, the Empire's Parliament; Marshal Deodoro da Fonseca, who as the senior military figure in the plot, assumed leadership of the movement, was supporter of the Conservative Party, and he took part in the coup because he was invited by other officers to lead the overthrowal of the Liberal Viscount of Ouro Preto from the Presidency of the Council, but although he intended to force a change of Prime Minister, initially Deodoro did not intend to depose Emperor Pedro II. Several of his co-conspirators, however, were Republicans, and later in the day the events of the military coup progressed to the deposition of the Monarchy. The decision to establish a republican Provisional Government was taken when Marshal Deodoro da Fonseca (who had already proclaimed "Long Live His Majesty the Emperor" during the public acts of the coup) received from his republican co-conspirator Benjamin Constant Botelho de Magalhães the false news that the Emperor intended to appoint Gaspar da Silveira Martins, a declared enemy of Marshal Deodoro da Fonseca, as the next Prime Minister in the Viscount of Ouro Preto's stead.
Once the Republic was proclaimed, a presidential Executive replaced the parliamentary system of Government.
President of the Council of Ministers of the United States of Brazil (1961–1963)[edit]
Prime Minister of United States of Brazil
Coat of arms
Residence
Brasília, Brazil
Appointer
President of Brazil (1961–1963)
Formation
7 September 1961
First holder
Tancredo Neves
Final holder
Hermes Lima
Abolished
23 January 1963
After the coup d'état that abolished the monarchy and proclaimed Brazil a republic, the system of parliamentary government was not retained. The new republic instead adopted the model of a presidential executive, except for a brief period (September 7, 1961 to January 23, 1963) during the presidency of President João Goulart.
The parliamentary system was adopted in 1961 as a compromise solution to a grave political crisis, and was again abolished, this time by plebiscite, in January 1963.
The official title of the head of the government during that period was President of the Council of Ministers, the same official title possessed by the 19th-century prime ministers of the Brazilian Empire. However, the holders of the office were informally addressed and referred to as Premier or Prime Minister. Often, the expression President of the Council, a simplified version of the official title, was also used.
List of Presidents of the Council of Ministers of the United States of Brazil[edit]
Parties
Social Democratic Party
Brazilian Socialist Party
#
Name
Portrait
Took office
Left office
Party
1 Tancredo de Almeida Neves 8 September 1961 12 July 1962 Social Democratic Party
2 Francisco de Paula Brochado da Rocha 12 July 1962 18 September 1962 Social Democratic Party
3 Hermes Lima 18 September 1962 23 January 1963 Brazilian Socialist Party
Timeline[edit]
Prime Ministers of Brazil (1847–1889) [show]
Prime Ministers of Brazil (1961–1963) [show]
See also[edit]
Wikimedia Commons has media related to Prime ministers of Brazil.
List of Brazilian monarchs
List of Presidents of Brazil
President of Brazil
References[edit]
Jump up ^ Nabuco, Joaquim (1975). Um Estadista do Império. único (4 ed.). Rio de Janeiro: Nova Aguilar, p. 712
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