RT Journal Article
SR Electronic
T1 A Panel of Monoclonal Antibodies Targeting the Rabies Virus Phosphoprotein Identifies a Highly Variable Epitope of Value for Sensitive Strain Discrimination
JF Journal of Clinical Microbiology
JO J. Clin. Microbiol.
FD American Society for Microbiology
SP 1397
OP 1403
DO 10.1128/JCM.38.4.1397-1403.2000
VO 38
IS 4
A1 Nadin-Davis, S. A.
A1 Sheen, M.
A1 Abdel-Malik, M.
A1 Elmgren, L.
A1 Armstrong, J.
A1 Wandeler, A. I.
YR 2000
UL http://jcm.asm.org/content/38/4/1397.abstract
AB A recombinant rabies virus phosphoprotein fusion product (GST-P) was used to generate a series of monoclonal antibodies (MAbs) with anti-P reactivity. Competitive binding assays classified 27 of these MAbs into four groups (I to IV), and 24 of them were deemed to recognize linear epitopes, as judged by their reaction in immunoblots. The linear epitope recognized in each case was mapped by using two series of N- and C-terminally deleted recombinant phosphoproteins. Assessment of the reactivities of representative MAbs to a variety of lyssavirus isolates by an indirect fluorescent antibody test indicated that group I MAbs, which recognized a highly conserved N-terminal epitope, were broadly cross-reactive with all lyssaviruses assayed, while group III MAbs, which reacted with a site overlapping that of group I MAbs, exhibited variable reactivities and group IV MAbs reacted with most isolates of genotypes 1, 6, and 7 only. In contrast, group II MAbs, which recognized an epitope located within a highly divergent central portion of the protein, were exquisitely strain specific. These anti-P MAbs are potentially useful tools for lyssavirus identification and discrimination.