Literature DB >> 7526825

Monoclonal antibodies reactive with specific amino acid sequences of the 126 K protein of tobacco mosaic virus.

P Das1, V Hari.   

Abstract

The 126 K protein of tobacco mosaic virus (TMV) is an NTP binding protein that has guanylyl transferase activity and is predicted to be an ATPase/helicase. In this paper we report the generation of monoclonal antibodies (Mabs) that react with specific amino acid sequences of the 126K protein. The Mabs were generated after immunizing mice with a partially purified preparation of the 126 K protein (native) obtained by centrifugal fractionation of the infected tissue extracts. The Mabs were assayed for specific reactivity by western blotting and by their reactivity with non-overlapping decapeptides corresponding to the entire amino acid sequence of the 126 K protein of TMV. A total of 11 Mabs reactive with specific peptides and three other Mabs that did not react with any peptide but reacted with the 126 K protein were identified.

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Year:  1994        PMID: 7526825     DOI: 10.1007/bf01311185

Source DB:  PubMed          Journal:  Arch Virol        ISSN: 0304-8608            Impact factor:   2.574


  10 in total

1.  Antigenic cross-reactivity potential of synthetic peptides immobilized on polyethylene rods.

Authors:  E Trifilieff; M C Dubs; M H Van Regenmortel
Journal:  Mol Immunol       Date:  1991-08       Impact factor: 4.407

2.  General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids.

Authors:  R A Houghten
Journal:  Proc Natl Acad Sci U S A       Date:  1985-08       Impact factor: 11.205

3.  Rapid "tea-bag" peptide synthesis using 9-fluorenylmethoxycarbonyl (Fmoc) protected amino acids applied for antigenic mapping of viral proteins.

Authors:  M Sällberg; U Rudén; L O Magnius; E Norrby; B Wahren
Journal:  Immunol Lett       Date:  1991-09       Impact factor: 3.685

Review 4.  Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids.

Authors:  G B Fields; R L Noble
Journal:  Int J Pept Protein Res       Date:  1990-03

5.  Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid.

Authors:  H M Geysen; R H Meloen; S J Barteling
Journal:  Proc Natl Acad Sci U S A       Date:  1984-07       Impact factor: 11.205

Review 6.  Antibody production by hybridomas.

Authors:  J W Goding
Journal:  J Immunol Methods       Date:  1980       Impact factor: 2.303

7.  Capping of tobacco mosaic virus RNA. Analysis of viral-coded guanylyltransferase-like activity.

Authors:  D D Dunigan; M Zaitlin
Journal:  J Biol Chem       Date:  1990-05-15       Impact factor: 5.157

8.  Photoaffinity labeling of a viral induced protein from tobacco. Characterization of nucleotide-binding properties.

Authors:  R K Evans; B E Haley; D A Roth
Journal:  J Biol Chem       Date:  1985-06-25       Impact factor: 5.157

9.  An analysis of tobacco mosaic virus replicative structures synthesized in vitro.

Authors:  N D Young; M Zaitlin
Journal:  Plant Mol Biol       Date:  1986-11       Impact factor: 4.076

10.  An NTP-binding motif is the most conserved sequence in a highly diverged monophyletic group of proteins involved in positive strand RNA viral replication.

Authors:  A E Gorbalenya; V M Blinov; A P Donchenko; E V Koonin
Journal:  J Mol Evol       Date:  1989-03       Impact factor: 2.395

  10 in total
  1 in total

1.  The GPRLQPY motif located at the carboxy-terminal of the spike protein induces antibodies that neutralize Porcine epidemic diarrhea virus.

Authors:  Deu John M Cruz; Chul-Joong Kim; Hyun-Jin Shin
Journal:  Virus Res       Date:  2007-12-11       Impact factor: 3.303

  1 in total

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