Literature DB >> 2430360

Tobacco mosaic virus coat protein and the large subunit of the host protein ribulose-1,5-biphosphate carboxylase share a common antigenic determinant.

R G Dietzgen, M Zaitlin.   

Abstract

An immunological relationship was detected between the coat protein of the common (U1) strain of tobacco mosaic virus (TMV) and the large subunit of the ubiquitous CO2-fixing host enzyme, ribulose-1,5-biphosphate carboxylase (RuBisCo). When assayed by Western immunoblotting or indirect ELISA, polyclonal antisera to TMV coat protein and to RuBisCo reacted with both antigens. In addition, a monoclonal antibody specific for the C-terminal antigenic determinant of TMV coat protein reacted with RuBisCo. Conversely, several monoclonal antibodies generated to the large subunit of RuBisCo reacted with TMV coat protein. This cross-reactivity was verified by an examination of the amino acid sequences of both proteins. A region of homology was found between the carboxy proximal portion of coat protein and the sequence 60-73 residues from the amino terminus of RuBisCo large subunit. This homology was not mirrored at the nucleic acid level because of different codon usages for the two proteins.

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Year:  1986        PMID: 2430360     DOI: 10.1016/0042-6822(86)90186-8

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  4 in total

1.  Solubilization of ribulose-1,5-bisphosphate carboxylase from the membrane fraction of pea leaves.

Authors:  A Makino; B Osmond
Journal:  Photosynth Res       Date:  1991-08       Impact factor: 3.573

2.  The Protective Effects of VVN001 on LPS-Induced Inflammatory Responses in Human RPE Cells and in a Mouse Model of EIU.

Authors:  Ruiqi Qiu; Mingzhu Yang; Weiping Wang; Jingyang Liu; Lin Yang; Bo Lei
Journal:  Inflammation       Date:  2020-11-16       Impact factor: 4.092

3.  Characterization of Thylakoid-Derived Lipid-Protein Particles Bearing the Large Subunit of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase.

Authors:  M. D. Smith; S. Ghosh; E. B. Dumbroff; J. E. Thompson
Journal:  Plant Physiol       Date:  1997-11       Impact factor: 8.340

4.  Spurious cross-reactions between plant viruses and monoclonal antibodies can be overcome by saturating ELISA plates with milk proteins.

Authors:  D Zimmermann; M H Van Regenmortel
Journal:  Arch Virol       Date:  1989       Impact factor: 2.574

  4 in total

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