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Papers by Erling Norrby

Research paper thumbnail of Serum Antibody Responses to Individual Viral Polypeptides in Human Rotavirus Infections

Journal of General Virology, 1987

A radioimmunoprecipitation assay (RIPA) was used to study the serum antibody responses to individ... more A radioimmunoprecipitation assay (RIPA) was used to study the serum antibody responses to individual polypeptides that developed after infection with viruses from human rotavirus subgroups I and II. Paired sera from eight children (1 to 8.5 years of age) were used in the study. Although all of the eight acute sera were negative by the complement fixation test, four of them were positive by RIPA, indicating a previous infection by rotavirus. A significant difference in the number of polypeptides immunoprecipitated was seen among the convalescent sera. The number of polypeptides immunoprecipitated was found to be related to previous infection experience. At most, ten different polypeptides were immunoprecipitated: seven structural polypeptides VPl to VP7 and three non-structural polypeptides, NSl, NS 2 and NS3. No sera immunoprecipitated VP8 or VP9. Acute sera positive by RIPA immunoprecipitated up to five polypeptides, VP1, VP2, VP3, VP4 and VP6. One of the non-structural proteins (NS2) was found to be particularly immunogenic, since antibodies to this polypeptide were detected in several convalescent sera. Among the structural proteins VP2 and VP6 were found to be the two immunodominant polypeptides which were recognized by all convalescent sera. Only three convalescent sera immunoprecipitated VP7, the major type-specific antigen responsible for inducing neutralizing antibodies. Three of four originally seronegative children with no reactivity in the convalescent sera to VP7 developed neutralizing antibodies to a single serotype. One child developed antibodies to two serotypes. 0000-7434 © 1987 SGM

Research paper thumbnail of Protection of hamsters against experimental mumps virus (MuV) infection by antibodies raised against the MuV surface glycoproteins expressed from recombinant vaccinia virus vectors

Journal of General Virology, 1995

The fusion (F) and haemagglutinin-neuraminidase (HN) glycoproteins of mumps virus (MuV) have been... more The fusion (F) and haemagglutinin-neuraminidase (HN) glycoproteins of mumps virus (MuV) have been produced in CV1 cells via vaccinia virus recombinants.

Research paper thumbnail of Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm

Virology, 1991

Measks virus (MV) proteins were efficiently expressed in COS and Vero cells from vectors baaed on... more Measks virus (MV) proteins were efficiently expressed in COS and Vero cells from vectors baaed on the strong cytomegeiovirus enhancer-promoter and protein(N) migrates predominantly into the nu sion of N and P proteins results in rete e to specific in had no effect P was suffiiie required for retention of N in the cytoplasm. Thus, the V and C proteins encoded within the first half of the P g#ne are not invoiced in the cytopleamic retantion of N protein. N protein might be fortuitously targeted to the nIjalews a&& ~a)euft of its many basic amino acids, presumably destined to interact with the MV genome. However, this set of experkents has allowed to analyze in viva the interactions between the N and P proteins.

Research paper thumbnail of Serum Antibody Responses to Individual Viral Polypeptides in Human Rotavirus Infections

Journal of General Virology, 1987

A radioimmunoprecipitation assay (RIPA) was used to study the serum antibody responses to individ... more A radioimmunoprecipitation assay (RIPA) was used to study the serum antibody responses to individual polypeptides that developed after infection with viruses from human rotavirus subgroups I and II. Paired sera from eight children (1 to 8.5 years of age) were used in the study. Although all of the eight acute sera were negative by the complement fixation test, four of them were positive by RIPA, indicating a previous infection by rotavirus. A significant difference in the number of polypeptides immunoprecipitated was seen among the convalescent sera. The number of polypeptides immunoprecipitated was found to be related to previous infection experience. At most, ten different polypeptides were immunoprecipitated: seven structural polypeptides VPl to VP7 and three non-structural polypeptides, NSl, NS 2 and NS3. No sera immunoprecipitated VP8 or VP9. Acute sera positive by RIPA immunoprecipitated up to five polypeptides, VP1, VP2, VP3, VP4 and VP6. One of the non-structural proteins (NS2) was found to be particularly immunogenic, since antibodies to this polypeptide were detected in several convalescent sera. Among the structural proteins VP2 and VP6 were found to be the two immunodominant polypeptides which were recognized by all convalescent sera. Only three convalescent sera immunoprecipitated VP7, the major type-specific antigen responsible for inducing neutralizing antibodies. Three of four originally seronegative children with no reactivity in the convalescent sera to VP7 developed neutralizing antibodies to a single serotype. One child developed antibodies to two serotypes. 0000-7434 © 1987 SGM

Research paper thumbnail of Protection of hamsters against experimental mumps virus (MuV) infection by antibodies raised against the MuV surface glycoproteins expressed from recombinant vaccinia virus vectors

Journal of General Virology, 1995

The fusion (F) and haemagglutinin-neuraminidase (HN) glycoproteins of mumps virus (MuV) have been... more The fusion (F) and haemagglutinin-neuraminidase (HN) glycoproteins of mumps virus (MuV) have been produced in CV1 cells via vaccinia virus recombinants.

Research paper thumbnail of Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm

Virology, 1991

Measks virus (MV) proteins were efficiently expressed in COS and Vero cells from vectors baaed on... more Measks virus (MV) proteins were efficiently expressed in COS and Vero cells from vectors baaed on the strong cytomegeiovirus enhancer-promoter and protein(N) migrates predominantly into the nu sion of N and P proteins results in rete e to specific in had no effect P was suffiiie required for retention of N in the cytoplasm. Thus, the V and C proteins encoded within the first half of the P g#ne are not invoiced in the cytopleamic retantion of N protein. N protein might be fortuitously targeted to the nIjalews a&& ~a)euft of its many basic amino acids, presumably destined to interact with the MV genome. However, this set of experkents has allowed to analyze in viva the interactions between the N and P proteins.

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