INHIBITION OF CELL-ADHESION TO THE VIRUS BY SYNTHETIC PEPTIDES OF FIBER KNOB OF HUMAN ADENOVIRUS SEROTYPE-2 AND SEROTYPE-3 AND VIRUS NEUTRALIZATION BY ANTIPEPTIDE ANTIBODIES
H. Liebermann et al., INHIBITION OF CELL-ADHESION TO THE VIRUS BY SYNTHETIC PEPTIDES OF FIBER KNOB OF HUMAN ADENOVIRUS SEROTYPE-2 AND SEROTYPE-3 AND VIRUS NEUTRALIZATION BY ANTIPEPTIDE ANTIBODIES, Virus research, 45(2), 1996, pp. 111-122
The fiber knob of adenovirus (Ad) causes the first step in the interac
tion of adenovirus with cell membrane receptors. To obtain information
on the receptor binding site(s) several synthetic peptides derived fr
om Ad2 and Ad3 fiber head sequences and their antisera were tested for
interference with virus attachment to HeLa and FL cells and cell adhe
sion to viruses. The anti-peptide sera were also evaluated in ELISA an
d virus neutralisation test. Ad2 (of subgroup C) and Ad3 (of subgroup
B) attachment was not significantly inhibited by peptides correspondin
g to the amino acid residues 535-554, 555-573, 562-582 of Ad2 fiber or
210-225, 267-283, 291-306 and 300-319 of Ad3 fiber. However, micropla
te pre-adsorbed Ad3 fiber residues 210-225 and 267-283 could bind FL a
nd HeLa cells, and 1 mg/ml of Ad3 fiber residues 267-283 inhibited the
cell adhesion to Ad3 virus to approximately 90%. This peptide may par
ticipate in the receptor binding site of Ad3 fiber. ELISA reactive ant
i-peptide antibodies against the homologous peptide and virus did not
significantly reduce the cell adhesion to the immobilised virus or the
virus attachment to cells: but in the neutralisation assay antibodies
raised to Ad2 fiber residues 555-573 and 562-582 and Ad3 fiber residu
es 210-225 caused neutralisation of the homologous virus at serum dilu
tions of 1:500 and 1:32, respectively. The corresponding peptides and
one further peptide of Ad2 fiber and two of Ad3 fiber seem to contain
neutralisation epitopes.