A malaria merozoite surface protein (MSP1)-structure, processing and function
Autor(a) principal: | |
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Data de Publicação: | 1992 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Memórias do Instituto Oswaldo Cruz |
Texto Completo: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000700004 |
Resumo: | Merozoite surface protein-1 (MSP-1, also referred to as P195, PMMSA or MSA 1) is one of the most studied of all malaria proteins. The proteins. The protein is found in all malaria species investigated and structural studies on the gene indicate that parts of the molecule are well-conserved. Studies on Plasmodium falciparum have shown that the protein is in a processed form on the merozoite surface, a result of proteolytic cleavage of the large percursor molecule. Recent studies have identified some of these cleavage sites. During invasion of the new red cell most of the MSP1 molecule is shed from the parasite surface except for a small C-terminal fragment which can be detected in ring stages. Analysis of the structure of this fragment suggests that it contains two growth factor-like domains that may have a functional role. |
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Memórias do Instituto Oswaldo Cruz |
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A malaria merozoite surface protein (MSP1)-structure, processing and functionmalariamerozoite surface proteinPlasmodiumMerozoite surface protein-1 (MSP-1, also referred to as P195, PMMSA or MSA 1) is one of the most studied of all malaria proteins. The proteins. The protein is found in all malaria species investigated and structural studies on the gene indicate that parts of the molecule are well-conserved. Studies on Plasmodium falciparum have shown that the protein is in a processed form on the merozoite surface, a result of proteolytic cleavage of the large percursor molecule. Recent studies have identified some of these cleavage sites. During invasion of the new red cell most of the MSP1 molecule is shed from the parasite surface except for a small C-terminal fragment which can be detected in ring stages. Analysis of the structure of this fragment suggests that it contains two growth factor-like domains that may have a functional role.Instituto Oswaldo Cruz, Ministério da Saúde1992-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000700004Memórias do Instituto Oswaldo Cruz v.87 suppl.3 1992reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02761992000700004info:eu-repo/semantics/openAccessHolder,Anthony A.Blackman,Michael J.Burghaus,Petra A.Chappel,Jonathan A.Ling,Irene T.McCallum-Deighton,NeilShai,Shafriraeng2020-04-25T17:46:56Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:05:00.691Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue |
dc.title.none.fl_str_mv |
A malaria merozoite surface protein (MSP1)-structure, processing and function |
title |
A malaria merozoite surface protein (MSP1)-structure, processing and function |
spellingShingle |
A malaria merozoite surface protein (MSP1)-structure, processing and function Holder,Anthony A. malaria merozoite surface protein Plasmodium |
title_short |
A malaria merozoite surface protein (MSP1)-structure, processing and function |
title_full |
A malaria merozoite surface protein (MSP1)-structure, processing and function |
title_fullStr |
A malaria merozoite surface protein (MSP1)-structure, processing and function |
title_full_unstemmed |
A malaria merozoite surface protein (MSP1)-structure, processing and function |
title_sort |
A malaria merozoite surface protein (MSP1)-structure, processing and function |
author |
Holder,Anthony A. |
author_facet |
Holder,Anthony A. Blackman,Michael J. Burghaus,Petra A. Chappel,Jonathan A. Ling,Irene T. McCallum-Deighton,Neil Shai,Shafrira |
author_role |
author |
author2 |
Blackman,Michael J. Burghaus,Petra A. Chappel,Jonathan A. Ling,Irene T. McCallum-Deighton,Neil Shai,Shafrira |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Holder,Anthony A. Blackman,Michael J. Burghaus,Petra A. Chappel,Jonathan A. Ling,Irene T. McCallum-Deighton,Neil Shai,Shafrira |
dc.subject.por.fl_str_mv |
malaria merozoite surface protein Plasmodium |
topic |
malaria merozoite surface protein Plasmodium |
dc.description.none.fl_txt_mv |
Merozoite surface protein-1 (MSP-1, also referred to as P195, PMMSA or MSA 1) is one of the most studied of all malaria proteins. The proteins. The protein is found in all malaria species investigated and structural studies on the gene indicate that parts of the molecule are well-conserved. Studies on Plasmodium falciparum have shown that the protein is in a processed form on the merozoite surface, a result of proteolytic cleavage of the large percursor molecule. Recent studies have identified some of these cleavage sites. During invasion of the new red cell most of the MSP1 molecule is shed from the parasite surface except for a small C-terminal fragment which can be detected in ring stages. Analysis of the structure of this fragment suggests that it contains two growth factor-like domains that may have a functional role. |
description |
Merozoite surface protein-1 (MSP-1, also referred to as P195, PMMSA or MSA 1) is one of the most studied of all malaria proteins. The proteins. The protein is found in all malaria species investigated and structural studies on the gene indicate that parts of the molecule are well-conserved. Studies on Plasmodium falciparum have shown that the protein is in a processed form on the merozoite surface, a result of proteolytic cleavage of the large percursor molecule. Recent studies have identified some of these cleavage sites. During invasion of the new red cell most of the MSP1 molecule is shed from the parasite surface except for a small C-terminal fragment which can be detected in ring stages. Analysis of the structure of this fragment suggests that it contains two growth factor-like domains that may have a functional role. |
publishDate |
1992 |
dc.date.none.fl_str_mv |
1992-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000700004 |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000700004 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0074-02761992000700004 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
dc.source.none.fl_str_mv |
Memórias do Instituto Oswaldo Cruz v.87 suppl.3 1992 reponame:Memórias do Instituto Oswaldo Cruz instname:Fundação Oswaldo Cruz instacron:FIOCRUZ |
reponame_str |
Memórias do Instituto Oswaldo Cruz |
collection |
Memórias do Instituto Oswaldo Cruz |
instname_str |
Fundação Oswaldo Cruz |
instacron_str |
FIOCRUZ |
institution |
FIOCRUZ |
repository.name.fl_str_mv |
Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz |
repository.mail.fl_str_mv |
|
_version_ |
1669937659552727040 |