Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2001-11-16
pubmed:abstractText
The envelope of human parainfluenza virus type 3 (HPF3) contains two viral glycoproteins, the hemagglutinin-neuraminidase (HN) protein and the fusion (F) protein. In a previous study, highly fusogenic variant HPF3 viruses were isolated, including two, C-0 and C-22, that exhibit increased avidity for sialic acid receptors due to single amino acid changes in the HN protein and one, C-28, that has decreased neuraminidase activity relative to that of the wild type (wt) and is delayed in the release of virus particles into the supernatant fluid. These variants form very large plaques and destroy a cell monolayer more rapidly than does wt HPF3 in cell culture. These variant viruses allowed us to formulate hypotheses about the roles of HN in pathogenesis. We investigated the behavior of wt HPF3 and the three variant viruses in the cotton rat model. In the cotton rat, there was no delayed clearance of any of the variant viruses compared to that of the wt. The variant plaque morphology was preserved in vivo, and there was no reversion to the wt phenotype in the infected animals. In spite of a slight advantage of wt virus in viral titer, there were no differences in the severities of peribronchiolitis between wt viruses and the variants. However, there were marked differences in severities in alveolitis and interstitial pneumonitis when each of the three variants was compared to the wt, with the variants causing enhanced disease. Thus, despite similar or lower viral titers and similar clearance rates, the variants caused more extensive disease in the lung. The results show that mutations in HN conferring altered fusion properties in cell culture also confer striking differences in the ability of HPF3 to cause extensive disease in the cotton rat lung and that this effect is dissociated from any effect on viral replication.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-10576209, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-10603317, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-11062565, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-11070006, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-11228376, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-11462020, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-1310764, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-1328668, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-1602561, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-1641990, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-1845878, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-1851852, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-2052599, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-3553614, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-3907188, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-6620458, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-7815489, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-8212546, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-8411349, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-8413475, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-8502295, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-8525632, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-8627023, http://linkedlifedata.com/resource/pubmed/commentcorrection/11711635-8965678
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12446-51
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Contribution of the human parainfluenza virus type 3 HN-receptor interaction to pathogenesis in vivo.
pubmed:affiliation
Virion Systems, Inc., Rockville, Maryland, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.