Abstract:
:Nonenveloped viral capsids are metastable structures that undergo conformational changes during virus entry that lead to interactions of the capsid or capsid fragments with the cell membrane. For members of the Caliciviridae, neither the nature of these structural changes in the capsid nor the factor(s) responsible for inducing these changes is known. Feline junctional adhesion molecule A (fJAM-A) mediates the attachment and infectious viral entry of feline calicivirus (FCV). Here, we show that the infectivity of some FCV isolates is neutralized following incubation with the soluble receptor at 37 degrees C. We used this property to select mutants resistant to preincubation with the soluble receptor. We isolated and sequenced 24 soluble receptor-resistant (srr) mutants and characterized the growth properties and receptor-binding activities of eight mutants. The location of the mutations within the capsid structure of FCV was mapped using a new 3.6-A structure of native FCV. The srr mutations mapped to the surface of the P2 domain were buried at the protruding domain dimer interface or were present in inaccessible regions of the capsid protein. Coupled with data showing that both the parental FCV and the srr mutants underwent increases in hydrophobicity upon incubation with the soluble receptor at 37 degrees C, these findings indicate that FCV likely undergoes conformational change upon interaction with its receptor. Changes in FCV capsid conformation following its interaction with fJAM-A may be important for subsequent interactions of the capsid with cellular membranes, membrane penetration, and genome delivery.
journal_name
J Viroljournal_title
Journal of virologyauthors
Ossiboff RJ,Zhou Y,Lightfoot PJ,Prasad BV,Parker JSdoi
10.1128/JVI.02371-09subject
Has Abstractpub_date
2010-06-01 00:00:00pages
5550-64issue
11eissn
0022-538Xissn
1098-5514pii
JVI.02371-09journal_volume
84pub_type
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journal_title:Journal of virology
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doi:10.1128/JVI.00557-12
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journal_title:Journal of virology
pub_type: 杂志文章
doi:10.1128/JVI.79.8.5047-5058.2005
更新日期:2005-04-01 00:00:00
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journal_title:Journal of virology
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journal_title:Journal of virology
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更新日期:1988-03-01 00:00:00
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journal_title:Journal of virology
pub_type: 杂志文章
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abstract::Rinderpest virus is a morbillivirus and is the causative agent of a widespread and important disease of cattle. The viral genome is a single strand of RNA in the negative sense. We have constructed plasmids containing cDNA copies of the 5' and 3' termini of the virus separated by a reporter gene and have shown that an...
journal_title:Journal of virology
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pub_type: 杂志文章
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abstract::Vif counteracts the host restriction factor APOBEC3G (A3G) and other APOBEC3s by preventing the incorporation of A3G into progeny virions. We previously identified Vif mutants with a dominant-negative (D/N) phenotype that interfered with the function of wild-type Vif, inhibited the degradation of A3G, and reduced the ...
journal_title:Journal of virology
pub_type: 杂志文章
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abstract:UNLABELLED:A balance between the functions of the influenza virus surface proteins hemagglutinin (HA) and neuraminidase (NA) is thought to be important for the transmission of viruses between humans. Here we describe two pandemic H1N1 viruses, A/swine/Virginia/1814-1/2012 and A/swine/Virginia/1814-2/2012 (pH1N1low-1 an...
journal_title:Journal of virology
pub_type: 杂志文章
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更新日期:2015-06-01 00:00:00