Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2011-7-28
pubmed:abstractText
Two WSSV envelope proteins, VP31 and VP33, contain a conserved Arg-Gly-Asp (RGD) sequence. In order to investigate the role of the RGD motif, wild-type and RGD-mutated VP31 and VP33 were recombinantly expressed in E. coli. The cell adhesion ability of the proteins was investigated in crayfish haemocytes using a fluorescence assay. The results showed that recombinant wild-type VP31 and VP33 had cell adhesion activity, and the RGD motif in VP31 was required for cell adhesion, which could be inhibited by an RGDT peptide. In contrast, the interaction of VP33 with cells did not require the RGD motif. These data indicate that the RGD motif plays an important role in the interaction between VP31 and host cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1432-8798
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
156
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1317-21
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
The RGD motif in VP31 of white spot syndrome virus is involved in cell adhesion.
pubmed:affiliation
Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, SOA, Xiamen, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't