Linked Life Data

15819601

Source:http://linkedlifedata.com/resource/pubmed/id/15819601

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-8-29
pubmed:abstractText
Native fluorescence spectroscopy (NFS), primarily from tryptophan (trp), was used for in situ investigation of the virus-receptor attachment process in phi6, a lipid-containing bacteriophage from the Cystoviridae family. NFS allowed us to monitor the viral attachment directly to its receptor, which was isolated from the pseudomonad host. Immediately upon mixing, an increase in tryptophan emission intensity was observed followed by a subsequent decrease in emission intensity. The initial increase in emission intensity reflects changes in trp quantum efficiency as the phi6 surface proteins change their conformation as a result of virus attachment to the pilus. The cystovirus spike protein P3 is responsible for receptor recognition and the fluorescence changes observed are likely to be the consequence of its conformational transition at this initial infection stage, providing a kinetic view of this process. The subsequent decrease in trp emission intensity could be due to changes in viral proteins as a result of disassembly of the pili. The technique may have important applications for the dynamic monitoring of additional stages of the virus replication cycle such as assembly, interaction with nucleic acids and maturation. This work expands on a previous demonstration that fluorescence offered a novel tool to detect virus particle interaction with its host cell.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0031-8655
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
879-83
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:articleTitle
Virus particles and receptor interaction monitored by fluorescence spectroscopy.
pubmed:affiliation
Institute for Ultrafast Spectroscopy and Lasers, The City College of New York, NY 10031, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural