Staphylococcal protein A-sepharose columns and the characterization of measles virus-specific polypeptides in persistently infected cells

Hayes, Edward C.; Wright, Larry L.; Zweerink, Hans J.

doi:10.1016/0003-2697(78)90841-2

Cited by 11 publications

(11 citation statements)

References 13 publications

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“…The presence of carbohydrate in the 48K protein further confirms that this polypeptide is not actin, a protein of similar Mr which is abundant in cell extracts and has a strong tendency to bind to Protein A-containing immunosorbents (Hayes et al, 1978) (Fig. 1, lanes 1, 7, 11 and 13).…”

Section: Glycosylation Of 56k To 58k and 48k Polypeptides Recognized mentioning

confidence: 55%

Neutralizing Monoclonal Antibodies to Bovine Viral Diarrhoea Virus Bind to the 56K to 58K Glycoprotein

Donis

Corapi

Dubovi

1988

Journal of General Virology

168

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SUMMARYA panel of murine monoclonal antibodies (MAbs) against the two major glycoproteins of bovine viral diarrhoea virus (BDV) was produced and assayed by serum neutralization, radioimmunoprecipitation (RIP) and immunoblotting. Based on their viral polypeptide specificity and on their ability to neutralize viral infectivity, the MAbs in the panel were divided into three classes : Class 1 MAbs reacted with the 56K to 58K glycoprotein and neutralized the virus, class 2 MAbs recognized the 56K to 58K glycoprotein but were not neutralizing, and class 3 MAbs reacted with the 48K glycoprotein and did not neutralize the virus. These results identify the 56K to 58K protein as one of the envelope glycoproteins of BDV. Evidence was obtained indicating that it is responsible for the induction of neutralizing antibodies. No large uncleared precursors of the 56K to 58K protein could be identified unequivocally by RIP of infected cell extracts, suggesting that this polypeptide is proteolytically processed cotranslationally. A subset of MAbs that reacted with BDV isolates of the noncytopathic biotypes yielded similar results, indicating that these findings are applicable to both biotypes of BDV.

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Section: Glycosylation Of 56k To 58k and 48k Polypeptides Recognized mentioning

confidence: 55%

Neutralizing Monoclonal Antibodies to Bovine Viral Diarrhoea Virus Bind to the 56K to 58K Glycoprotein

Donis

Corapi

Dubovi

1988

Journal of General Virology

168

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“…l b, lanes 5 to 8), two host-coded proteins that migrated close to GP46 were observed. The smaller of the two is probably actin (Hayes et al, 1978). The recoveries of radioactivity in the immunoprecipitates of infected cells shown in lanes 5 and 7 of Fig.…”

Section: Identification Of Den-2 Virus-specified Proteins and Glycoprmentioning

confidence: 84%

Synthesis of Proteins and Glycoproteins in Dengue Type 2 Virus-infected Vero and Aedes albopictus Cells

Smith

Wright

1985

Journal of General Virology

138

102

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SUMMARYFifteen proteins were detected in Vero cells infected by dengue type 2 (DEN-2) virus that were not observed in mock-infected cells, namely P98, p82, P67, GP60, gp54, GP46, p30, p28, gp22, GP20, pl8, gpl6, pl5, pl4 and gpl3. With the exceptions of gp54 and gp 13, polypeptides corresponding to those listed above were also observed in DEN-2 virus-infected Aedes albopictus C6/36 cells. Pulse-chase labelling experiments suggested a possible precursor product relationship between p30 and p28, and between gp22 and GP20. Peptide mapping and immunoprecipitation experiments showed that the major glycoproteins GP60, GP46 and GP20 were unrelated. Immunoprecipitations of infected ceils with antiserum prepared against the DEN-2 soluble complementfixing (SCF) antigen demonstrated that this antigen is equivalent to the non-structural glycoprotein GP46. The envelope glycoprotein (E) from virus grown in C6/36 cells migrated faster through polyacrylamide gels containing SDS than E from virus grown in Vero cells.[3H]Mannose-labelled glycopeptides of GP60, GP46 and GP20 were separated by gel filtration and by electrophoresis in Tris-borate gels; in addition, the polypeptides synthesized in infected cells in the presence of tunicamycin were analysed. The results revealed heterogeneity among the glycan units of GP60 and GP46.

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“…The Staph A, with adsorbed immune complexes, was washed four times with TDSET. The labeled, precipitated antigens were eluted by resuspending the Staph A pellet in 30/~1 of 0.1 M Tris-HCl (pH 6.8), 2% (wt/vol) SDS, 20% (vol/vol) glycerol, 2% (wt/vol) fl-mercaptoethanol, and 0.02% (wt/vol) bromophenol blue (SP buffer) (31) and boiling the suspension for 3 min. The Staph A was pelleted and the supernatant was subjected to SDS-polyacrylamide gel electrophoresis (PAGE).…”

Section: Methodsmentioning

confidence: 99%

Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens.

Leith

Treviño

Tully

et al. 1983

The Journal of Experimental Medicine

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The immune response of experimentally infected hamsters and human patients to Mycoplasma pneumoniae was examined by radioimmunoprecipation in conjunction with gel electrophoresis and fluorography. Both intrinsically and extrinsically labeled mycoplasma proteins were coincubated with acute and convalescent sera in a radioimmunoprecipitation assay. Two M. pneumoniae proteins were selectively precipitated by convalescent sera. These predominant immunogens were trypsin-sensitive, antibody-accessible surface proteins that co-migrate on polyacrylamide gels with proteins P1 and P2, which were previously implicated by us as mediators of cytadsorption. Anti-M. pneumoniae antiserum did not precipitate radiolabeled antigens derived from Mycoplasma orale or Mycoplasma salivarium. These data indicate that M. pneumoniae infection stimulates a specific and highly targeted host antibody response to key proteinaceous immunogens.

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Staphylococcal protein A-sepharose columns and the characterization of measles virus-specific polypeptides in persistently infected cells

Cited by 11 publications

References 13 publications

Neutralizing Monoclonal Antibodies to Bovine Viral Diarrhoea Virus Bind to the 56K to 58K Glycoprotein

Neutralizing Monoclonal Antibodies to Bovine Viral Diarrhoea Virus Bind to the 56K to 58K Glycoprotein

Synthesis of Proteins and Glycoproteins in Dengue Type 2 Virus-infected Vero and Aedes albopictus Cells

Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens.

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