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Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily

Striking similarities between vaccinia virus hemagglutinin (VVHA) and proteins belonging to the Ig superfamily clearly indicate that VVHA, a 315-amino acid glycoprotein expressed on the surface of the infected cells, is a novel viral protein that can be added to the expanding list of the Ig superfam...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1989
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189399/
https://www.ncbi.nlm.nih.gov/pubmed/2754392
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description Striking similarities between vaccinia virus hemagglutinin (VVHA) and proteins belonging to the Ig superfamily clearly indicate that VVHA, a 315-amino acid glycoprotein expressed on the surface of the infected cells, is a novel viral protein that can be added to the expanding list of the Ig superfamily. Its deduced amino acid sequence contains one Ig- like domain at the NH2 terminus, followed by two tandem repeating units and a hydrophobic region, suggestive of membrane spanning. The results offer an opportunity for the further study of the probable evolutionary and possible functional relationship between VVHA and other members of the Ig superfamily. Our observation, together with a recent finding that human CMV possibly encodes a protein similar to the MHC class I antigens (13), provides evidence supporting the fact that the viral capture of cellular Ig-related genes is more common than expected in vaccinia and other viruses, and that usage of an Ig-like domain as recognition signals might be extended from higher animals to animal viruses.
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spelling pubmed-21893992008-04-17 Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily J Exp Med Articles Striking similarities between vaccinia virus hemagglutinin (VVHA) and proteins belonging to the Ig superfamily clearly indicate that VVHA, a 315-amino acid glycoprotein expressed on the surface of the infected cells, is a novel viral protein that can be added to the expanding list of the Ig superfamily. Its deduced amino acid sequence contains one Ig- like domain at the NH2 terminus, followed by two tandem repeating units and a hydrophobic region, suggestive of membrane spanning. The results offer an opportunity for the further study of the probable evolutionary and possible functional relationship between VVHA and other members of the Ig superfamily. Our observation, together with a recent finding that human CMV possibly encodes a protein similar to the MHC class I antigens (13), provides evidence supporting the fact that the viral capture of cellular Ig-related genes is more common than expected in vaccinia and other viruses, and that usage of an Ig-like domain as recognition signals might be extended from higher animals to animal viruses. The Rockefeller University Press 1989-08-01 /pmc/articles/PMC2189399/ /pubmed/2754392 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily
title Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily
title_full Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily
title_fullStr Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily
title_full_unstemmed Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily
title_short Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily
title_sort vaccinia virus hemagglutinin. a novel member of the immunoglobulin superfamily
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189399/
https://www.ncbi.nlm.nih.gov/pubmed/2754392