PMID: 8581013Jan 1, 1995Paper

Synthetic peptides reveal a phospholipid binding domain in the glycoprotein of VHSV, a salmonid rhabdovirus

Veterinary Research
J M Coll

Abstract

Using phosphatidylserine (PS) binding to solid-phase synthetic 15-aa peptides, which covered the full length glycoprotein G of a salmonid rhabdovirus, viral haemorrhagic septicaemia virus (VHSV), evidence is presented showing the mapping of its major phospholipid-binding region. Three overlapping peptides were the dominant but not exclusive, reactive peptides that defined the phospholipid-binding main region. A 28-aa synthetic peptide (p2, aa 82-109), defined by the sequences of the 3 above-mentioned peptides, contained a putative alpha-helix domain with 3 consecutive hydrophobic amino acid a-d heptad-repeats (amphipathic alpha-helix), and 2 arginines at its carboxy terminal part. This peptide showed a higher apparent specific activity of PS-binding than the 15-aa peptides. Only native, denatured or recombinant fragment G4 viral glycoprotein G showed PS-binding. This did not occur for any of the other VHSV proteins tested. The highest specific activity of PS-binding, however, was found for purified VHSV. PS-binding to purified VHSV was abolished by any VHSV treatment that removed the glycoprotein G from the virions and was partially inhibited by anti-p2 mouse antibodies. It was higher at pH 5.6 than at pH 7.6. The identificatio...Continue Reading

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