Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2007-6-13
pubmed:abstractText
Herpesviruses must traverse the nuclear envelope to gain access to the cytoplasm and, ultimately, to exit cells. It is believed that herpesvirus nucleocapsids enter the perinuclear space by budding through the inner nuclear membrane (NM). To reach the cytoplasm these enveloped particles must fuse with the outer NM and the unenveloped capsids then acquire a second envelope in the trans-Golgi network. Little is known about the process by which herpesviruses virions fuse with the outer NM. Here we show that a herpes simplex virus (HSV) mutant lacking both the two putative fusion glycoproteins gB and gH failed to cross the nuclear envelope. Enveloped virions accumulated in the perinuclear space or in membrane vesicles that bulged into the nucleoplasm (herniations). By contrast, mutants lacking just gB or gH showed only minor or no defects in nuclear egress. We concluded that either HSV gB or gH can promote fusion between the virion envelope and the outer NM. It is noteworthy that fusion associated with HSV entry requires the cooperative action of both gB and gH, suggesting that the two types of fusion (egress versus entry) are dissimilar processes.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-11264357, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-11356979, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-11507225, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-11799148, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-12161659, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-12857917, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-12970403, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-1309250, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-1309262, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-1318405, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-14671121, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-15140953, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-15140956, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-15189158, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-15389628, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-15613336, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-15709012, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-15890903, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-16103147, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-16415038, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-16537585, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-16775344, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-16775362, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-16814597, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-16840698, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-17299053, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-2833603, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-3010695, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-3027398, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-7636985, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-8189508, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-8383241, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-8642656, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-8645092, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-9094688, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-9292005, http://linkedlifedata.com/resource/pubmed/commentcorrection/17548810-9724605
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
104
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10187-92
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane.
pubmed:affiliation
Department of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, OR 97239, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural