A malaria merozoite surface protein (MSP1)-structure, processing and function

Detalhes bibliográficos
Autor(a) principal: Holder,Anthony A.
Data de Publicação: 1992
Outros Autores: Blackman,Michael J., Burghaus,Petra A., Chappel,Jonathan A., Ling,Irene T., McCallum-Deighton,Neil, Shai,Shafrira
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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spelling 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
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