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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1994-8-8
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pubmed:abstractText |
The virus yield of human parainfluenza virus type-1 (hPIV-1) in cultured cells at 38 degrees C is reduced more than 100-fold compared to 34 degrees C, while the virus yield of Sendai virus (SV, Enders strain), a murine parainfluenza virus type-1 with high homology to hPIV-1 was almost equal at both temperatures. To understand the basis for the differences in the temperature growth characteristics of the two viruses, we examined the heat-stability of hPIV-1 and SV glycoproteins expressed from cDNAs by pulse-chase experiments. The hemagglutinin-neuraminidase (HN) protein of hPIV-1 was stable after a 6-h chase at 34 degrees C, while at 38 degrees C prominent protein degradation was observed starting at 3 h chase and by 6 h HN was reduced by 65%. In contrast, SV HN protein was stable at both 34 and 38 degrees C. The other hPIV-1 glycoprotein, the fusion (F) protein was stable at both temperatures. To identify the amino acids which are responsible for the heat-lability of hPIV-1 HN, mutant HN proteins were constructed by site-directed mutagenesis. Mutant hPIV-1 HN which had substitutions at positions 461 and 462 became heat-stable at 38 degrees C. These data indicate amino acids around 461 are responsible for the heat-lability of the wild type hPIV-1 HN protein and the reduced yield of the virus at 38 degrees C.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0168-1702
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
85-92
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8030367-Amino Acid Sequence,
pubmed-meshheading:8030367-Cells, Cultured,
pubmed-meshheading:8030367-HN Protein,
pubmed-meshheading:8030367-Hot Temperature,
pubmed-meshheading:8030367-Humans,
pubmed-meshheading:8030367-Molecular Sequence Data,
pubmed-meshheading:8030367-Parainfluenza Virus 1, Human,
pubmed-meshheading:8030367-Protein Denaturation,
pubmed-meshheading:8030367-Virus Replication
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pubmed:year |
1994
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pubmed:articleTitle |
The human parainfluenza virus type-1 prototypic strain contains a heat-labile hemagglutinin-neuraminidase protein.
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pubmed:affiliation |
Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, TN 38101-0318.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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