File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Vaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily

TitleVaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamily
Authors
Issue Date1989
PublisherRockefeller University Press. The Journal's web site is located at http://www.jem.org
Citation
Journal Of Experimental Medicine, 1989, v. 170 n. 2, p. 571-576 How to Cite?
AbstractStriking 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 NH 2 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, 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 the usage of an Ig-like domain as recognition signals might be extended from higher animals to animal viruses.
Persistent Identifierhttp://hdl.handle.net/10722/147337
ISSN
2021 Impact Factor: 17.579
2020 SCImago Journal Rankings: 8.483
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorJin, Den_US
dc.contributor.authorLi, Zen_US
dc.contributor.authorJin, Qen_US
dc.contributor.authorYuwen, Hen_US
dc.contributor.authorHou, Yen_US
dc.date.accessioned2012-05-29T06:03:01Z-
dc.date.available2012-05-29T06:03:01Z-
dc.date.issued1989en_US
dc.identifier.citationJournal Of Experimental Medicine, 1989, v. 170 n. 2, p. 571-576en_US
dc.identifier.issn0022-1007en_US
dc.identifier.urihttp://hdl.handle.net/10722/147337-
dc.description.abstractStriking 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 NH 2 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, 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 the usage of an Ig-like domain as recognition signals might be extended from higher animals to animal viruses.en_US
dc.languageengen_US
dc.publisherRockefeller University Press. The Journal's web site is located at http://www.jem.orgen_US
dc.relation.ispartofJournal of Experimental Medicineen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshHemagglutinins, Viral - Geneticsen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMultigene Familyen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshSolubilityen_US
dc.subject.meshVaccinia Virus - Geneticsen_US
dc.subject.meshViral Proteins - Genetics - Ultrastructureen_US
dc.titleVaccinia virus hemagglutinin. A novel member of the immunoglobulin superfamilyen_US
dc.typeArticleen_US
dc.identifier.emailJin, D:dyjin@hkucc.hku.hken_US
dc.identifier.authorityJin, D=rp00452en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1084/jem.170.2.571-
dc.identifier.pmid2754392-
dc.identifier.scopuseid_2-s2.0-0024358772en_US
dc.identifier.volume170en_US
dc.identifier.issue2en_US
dc.identifier.spage571en_US
dc.identifier.epage576en_US
dc.identifier.isiWOS:A1989AK03400015-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridJin, D=7201973614en_US
dc.identifier.scopusauthoridLi, Z=24724591600en_US
dc.identifier.scopusauthoridJin, Q=35210232500en_US
dc.identifier.scopusauthoridYuwen, H=6506818196en_US
dc.identifier.scopusauthoridHou, Y=7402198565en_US
dc.identifier.issnl0022-1007-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats