Echinococcus granulosus antigen B structure: subunit composition and oligomeric states.
BACKGROUND: Antigen B (AgB) is the major protein secreted by the Echinococcus granulosus metacestode and is involved in key host-parasite interactions during infection. The full comprehension of AgB functions depends on the elucidation of several structural aspects that remain unknown, such as its s...
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ftdoajarticles:oai:doaj.org/article:9e76066647f348718e5475ce94fade34 2023-05-15T15:14:15+02:00 Echinococcus granulosus antigen B structure: subunit composition and oligomeric states. Karina M Monteiro Mateus B Cardoso Cristian Follmer Nádya P da Silveira Daiani M Vargas Elliot W Kitajima Arnaldo Zaha Henrique B Ferreira 2012-01-01T00:00:00Z https://doi.org/10.1371/journal.pntd.0001551 https://doaj.org/article/9e76066647f348718e5475ce94fade34 EN eng Public Library of Science (PLoS) http://europepmc.org/articles/PMC3295803?pdf=render https://doaj.org/toc/1935-2735 1935-2735 doi:10.1371/journal.pntd.0001551 https://doaj.org/article/9e76066647f348718e5475ce94fade34 PLoS Neglected Tropical Diseases, Vol 6, Iss 3, p e1551 (2012) Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 article 2012 ftdoajarticles https://doi.org/10.1371/journal.pntd.0001551 2022-12-31T06:26:32Z BACKGROUND: Antigen B (AgB) is the major protein secreted by the Echinococcus granulosus metacestode and is involved in key host-parasite interactions during infection. The full comprehension of AgB functions depends on the elucidation of several structural aspects that remain unknown, such as its subunit composition and oligomeric states. METHODOLOGY/PRINCIPAL FINDINGS: The subunit composition of E. granulosus AgB oligomers from individual bovine and human cysts was assessed by mass spectrometry associated with electrophoretic analysis. AgB8/1, AgB8/2, AgB8/3 and AgB8/4 subunits were identified in all samples analyzed, and an AgB8/2 variant (AgB8/2v8) was found in one bovine sample. The exponentially modified protein abundance index (emPAI) was used to estimate the relative abundance of the AgB subunits, revealing that AgB8/1 subunit was relatively overrepresented in all samples. The abundance of AgB8/3 subunit varied between bovine and human cysts. The oligomeric states formed by E. granulosus AgB and recombinant subunits available, rAgB8/1, rAgB8/2 and rAgB8/3, were characterized by native PAGE, light scattering and microscopy. Recombinant subunits showed markedly distinct oligomerization behaviors, forming oligomers with a maximum size relation of rAgB8/3>rAgB8/2>rAgB8/1. Moreover, the oligomeric states formed by rAgB8/3 subunit were more similar to those observed for AgB purified from hydatid fluid. Pressure-induced dissociation experiments demonstrated that the molecular assemblies formed by the more aggregative subunits, rAgB8/2 and rAgB8/3, also display higher structural stability. CONCLUSIONS/SIGNIFICANCE: For the first time, AgB subunit composition was analyzed in samples from single hydatid cysts, revealing qualitative and quantitative differences between samples. We showed that AgB oligomers are formed by different subunits, which have distinct abundances and oligomerization properties. Overall, our findings have significantly contributed to increase the current knowledge on AgB expression and ... Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic PLoS Neglected Tropical Diseases 6 3 e1551 |
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English |
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Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
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Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 Karina M Monteiro Mateus B Cardoso Cristian Follmer Nádya P da Silveira Daiani M Vargas Elliot W Kitajima Arnaldo Zaha Henrique B Ferreira Echinococcus granulosus antigen B structure: subunit composition and oligomeric states. |
topic_facet |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
description |
BACKGROUND: Antigen B (AgB) is the major protein secreted by the Echinococcus granulosus metacestode and is involved in key host-parasite interactions during infection. The full comprehension of AgB functions depends on the elucidation of several structural aspects that remain unknown, such as its subunit composition and oligomeric states. METHODOLOGY/PRINCIPAL FINDINGS: The subunit composition of E. granulosus AgB oligomers from individual bovine and human cysts was assessed by mass spectrometry associated with electrophoretic analysis. AgB8/1, AgB8/2, AgB8/3 and AgB8/4 subunits were identified in all samples analyzed, and an AgB8/2 variant (AgB8/2v8) was found in one bovine sample. The exponentially modified protein abundance index (emPAI) was used to estimate the relative abundance of the AgB subunits, revealing that AgB8/1 subunit was relatively overrepresented in all samples. The abundance of AgB8/3 subunit varied between bovine and human cysts. The oligomeric states formed by E. granulosus AgB and recombinant subunits available, rAgB8/1, rAgB8/2 and rAgB8/3, were characterized by native PAGE, light scattering and microscopy. Recombinant subunits showed markedly distinct oligomerization behaviors, forming oligomers with a maximum size relation of rAgB8/3>rAgB8/2>rAgB8/1. Moreover, the oligomeric states formed by rAgB8/3 subunit were more similar to those observed for AgB purified from hydatid fluid. Pressure-induced dissociation experiments demonstrated that the molecular assemblies formed by the more aggregative subunits, rAgB8/2 and rAgB8/3, also display higher structural stability. CONCLUSIONS/SIGNIFICANCE: For the first time, AgB subunit composition was analyzed in samples from single hydatid cysts, revealing qualitative and quantitative differences between samples. We showed that AgB oligomers are formed by different subunits, which have distinct abundances and oligomerization properties. Overall, our findings have significantly contributed to increase the current knowledge on AgB expression and ... |
format |
Article in Journal/Newspaper |
author |
Karina M Monteiro Mateus B Cardoso Cristian Follmer Nádya P da Silveira Daiani M Vargas Elliot W Kitajima Arnaldo Zaha Henrique B Ferreira |
author_facet |
Karina M Monteiro Mateus B Cardoso Cristian Follmer Nádya P da Silveira Daiani M Vargas Elliot W Kitajima Arnaldo Zaha Henrique B Ferreira |
author_sort |
Karina M Monteiro |
title |
Echinococcus granulosus antigen B structure: subunit composition and oligomeric states. |
title_short |
Echinococcus granulosus antigen B structure: subunit composition and oligomeric states. |
title_full |
Echinococcus granulosus antigen B structure: subunit composition and oligomeric states. |
title_fullStr |
Echinococcus granulosus antigen B structure: subunit composition and oligomeric states. |
title_full_unstemmed |
Echinococcus granulosus antigen B structure: subunit composition and oligomeric states. |
title_sort |
echinococcus granulosus antigen b structure: subunit composition and oligomeric states. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2012 |
url |
https://doi.org/10.1371/journal.pntd.0001551 https://doaj.org/article/9e76066647f348718e5475ce94fade34 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
PLoS Neglected Tropical Diseases, Vol 6, Iss 3, p e1551 (2012) |
op_relation |
http://europepmc.org/articles/PMC3295803?pdf=render https://doaj.org/toc/1935-2735 1935-2735 doi:10.1371/journal.pntd.0001551 https://doaj.org/article/9e76066647f348718e5475ce94fade34 |
op_doi |
https://doi.org/10.1371/journal.pntd.0001551 |
container_title |
PLoS Neglected Tropical Diseases |
container_volume |
6 |
container_issue |
3 |
container_start_page |
e1551 |
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1766344718967373824 |