Arch Virol (1999) 144: 1035–1039
A monoclonal antibody that recognizes the predicted tick-borne
encephalitis virus E protein fusion sequence blocks fusion
T. D. Volkova
, M. F. Vorovitch
, A. V. Timofeev
, and O. M. Volpina
Shimyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS,
Chumakov Institute of Poliomyelitis and Viral Encephalitides RAMS,
Accepted September 11, 1998
Summary. The fusion motif of tick-borne encephalitis virus E protein has been
predicted to be located within its conserved region (98–120). Results are
presented to demonstrate that non-neutralizing monoclonal antibody which
recognizes a synthetic peptide corresponding to residues 98–113 of the E protein
sequence can block the fusion of the virus particles with artiﬁcial membranes.
Tick-borne encephalitis (TBE) virus is a member of the Flaviviridae family of
enveloped viruses. The virions consist of 3 structural proteins-C, M and E. The
entrance of ﬂaviviruses into the cells during infection includes, in general, a
fusion process between virus and cellular membranes. It has been demonstrated
that structural rearrangements in envelope glycoprotein E of TBE virus at low
pH induce its fusion with cellular membranes [1, 6, 13]. Epitope mapping using
monoclonal antibodies has located the fusogenic region in the R1 domain of the
TBE viral E protein [6, 13]. Recently, this region has been clearly deﬁned in a
high resolution structural model of the TBE virus E protein .
In their analysis of the variable ﬂaviviral E protein R1 domain, Roehrig et al.
 suggested on the basis of its amino acid composition and chemical charac-
teristics that the extremely conserved region corresponding to residues 98–120
was the fusogenic motif of the protein.
In this paper it will be shown that a monoclonal antibody which recognizes
the synthetic peptide corresponding to the predicted fusogenic motive of TBE
virus can block the fusion process between the virus and artiﬁcial membranes.
Peptides 1–4 (Table 1) used in the study were synthesised manually using
Boc-solid-phase chemistry on the 4-(hydroxymethyl) phenylacetmidomethyl-