Antibodies to Respiratory Syncytial Virus Polypeptides and their Significance in Human Infection

Ward, Kevin; Lambden, Paul R.; Ogilvie, Marie M.; Watt, P. J.

doi:10.1099/0022-1317-64-9-1867

Cited by 121 publications

(94 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The calculated molecular weight for RS virus phosphoprotein deduced from the cDNA sequence data was 27166. This value was considerably less than the Mr 35000 estimated by SDS-PAGE (Ward et al, 1983). This type of aberrant behaviour on SDS-PAGE was also observed for the phosphorylated NS protein of VS virus (Gallione et al, 1981) and the P protein of Sendai virus (Giorgi et al, 1983).…”

mentioning

confidence: 71%

“…Recombinant cDNA clones were identified by in vitro translation of hybrid-selected mRNA using a rabbit reticulocyte lysate system (Parnes et al, 1981). Putative RS virus clones were confirmed by radioimmunoprecipitation of the in vitro translated proteins using specific RS virus monoclonal antibodies (Ward et al, 1983). In view of the significant human antibody response to RS virus phosphoprotein and the potential use of this major antigen in diagnostic tests, clones hybrid-selecting phosphoprotein mRNA were chosen for further study.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Nucleotide Sequence of the Respiratory Syncytial Virus Phosphoprotein Gene

Lambden

1985

Journal of General Virology

Self Cite

View full text Add to dashboard Cite

SUMMARYA cDNA library was prepared from poly(A) + RNA extracted from respiratory syncytial (RS) virus-infected HEp-2 cells. A recombinant plasmid, pRSP68, encoding the RS virus phosphoprotein gene was identified by translation in vitro of hybridselected mRNA. The cloned cDNA insert of 1 kb was sequenced and a polypeptide of 241 amino acids with a molecular weight of 27166 was deduced from the sequence. The protein was relatively rich in polar amino acids and devoid of both cysteine and tryptophan. A second short open reading frame with a coding potential of 65 amino acids was identified and overlapped the 3' terminus of the phosphoprotein gene by 34 bases.Respiratory syncytial (RS) virus is the major pathogen causing severe lower respiratory tract infection in infants (Parrott et al., 1973). The virus is a pleomorphic, unsegmented, negativestranded RNA virus similar to the paramyxoviruses but placed in a separate genus, Pneumovirus, on the basis of its morphology and the lack of detectable neuraminidase and haemagglutinin activities. More recently, study of the genetic organization of RS virus has highlighted the differences between it and the typical paramyxoviruses . The RS viral genome is a single negative strand of RNA with a molecular weight of around 5 × 106, and is transcribed into 10 discrete polyadenylated mRNAs coding for 10 unique viral proteins . The gene order has been determined by transcriptional mapping using u.v. inactivation kinetics (Dickens et al., 1984). These studies provided evidence of a single promoter site for RS virus transcription and the gene order:

show abstract

mentioning

confidence: 71%

mentioning

confidence: 99%

Nucleotide Sequence of the Respiratory Syncytial Virus Phosphoprotein Gene

Lambden

1985

Journal of General Virology

Self Cite

View full text Add to dashboard Cite

show abstract

“…The N protein is also highly conserved (> 99%) between two BRSV strains [1]. Serum samples from infected calves contain abundant N protein antibodies [24,25]. The BRSV N protein has been synthesized at high levels using the baculovirus expression system [16].…”

Section: Introductionmentioning

confidence: 99%

Bovine respiratory syncytial virus: first serological evidence in Uruguay

et al. 2000

View full text Add to dashboard Cite

-Bovine respiratory syncytial virus (BRSV) is a major cause of respiratory disease in calves resulting in a substantial economic loss for the cattle industry worldwide. In order to determine the presence of BRSV in Uruguay, an immunoenzymatic test was set up, using a recombinant BRSV nucleocapsid (N) protein as the antigen. The N protein was produced in Sf9 insect cells by a recombinant baculovirus expressing the N protein. Serum samples collected from one hundred cattle from four different geographic regions of Uruguay were analyzed. Antibodies against the N protein of BRSV were detected in 95% of the serum samples analyzed. These results show for the first time the presence of BRSV antibodies and suggest a widespread BRSV infection in the cattle population of Uruguay. respiratory syncytial virus / recombinant N protein / epidemiology / baculovirus / UruguayRésumé -Première mise en évidence sérologique du virus syncytial respiratoire bovin en Uruguay. Le virus syncytial respiratoire bovin (VSRB) est une cause majeure de maladie respiratoire chez le veau, provoquant des pertes économiques importantes pour l'industrie bovine dans le monde entier. Afin de mettre en évidence la présence du VSRB en Uruguay, un test immunoenzymatique a été élaboré, qui utilise comme antigène une protéine recombinante de nucléocapside (N) du VSRB. La protéine N a été produite dans des cellules d'insecte Sf9 par un baculovirus recombinant exprimant la protéine N. Des échantillons de sérum prélevés sur 100 bovins, provenant de quatre régions différentes d'Uruguay, ont été analysés. Des anticorps dirigés contre la protéine N du VSRB ont été détectés dans 95% des échantillons analysés. Ces résultats montrent, pour la première fois, la présence d'anticorps anti-VSRB et suggèrent que l'infection par le VSRB est largement répandue dans la population bovine en Uruguay. virus syncytial respiratoire bovin / protéine N recombinante / épidémiologie / baculovirus / Uruguay Vet. Res. 31 (2000) [241][242][243][244][245][246] 241

show abstract

“…Furthermore the footprinting analysis by proteolysis of MAb-bound anti-F proteins shows patterns of breakdown products characteristic of subtype A and B viruses. In studies of one RS virus strain from a local epidemic, Ward et al (1983) noted that their anti-F MAb immunoprecipitated a nonglycosylated 23K protein in addition to the glycopolypeptides F1 and F2. Judging from the present data it is likely that the epidemic studied was caused by a subtype A virus strain.…”

Section: E N O R R B Y M a M U F S O N A N D H S H E S H B E R mentioning

confidence: 99%

Structural Differences between Subtype A and B Strains of Respiratory Syncytial Virus

Norrby

Mufson

Sheshberadaran

1986

Journal of General Virology

View full text Add to dashboard Cite

SUMMARYDifferences in the properties of homologous intracellular structural components of eight strains of subtype A and eight strains of subtype B of human respiratory syncytial (RS) virus were examined. The size of the fusion (F) protein cleavage products and the phosphoprotein (P) showed systematic differences between virus strains representing the two subtypes. The apparent mol. wt. in SDS-polyacrylamide gels under reducing conditions was 48000 (48K) and 46K to 47K for the cleavage product FI in subtype A and B strains, respectively. The size of the F2 protein was 18K to 20K. The subtype B strains showed a slightly higher tool. wt. of this protein compared to the subtype A strains. The size of the P protein was 36K in subtype A strains, but only 34K in subtype B strains. Variations also occurred in the size of the glycoprotein (G) and the 22K to 24K structural protein. These variations did not correlate with the virus subtypes, but were strain-specific. The size of non-glycosylated forms of the F protein cleavage products was determined by use of material from tunicamycin-treated cells. A 44K to 45K non-glycosylated form of the F 1 protein was detected with subtype A virus strains, but the corresponding protein of subtype B strains was not reproducibly identified, presumably due to instability in the absence of glycosylation or altered antigenicity. Monoclonal antibody immunosorbent-bound viral glycoproteins were partially digested with proteases. The pattern of breakdown products of the F1 protein was distinctly different between subtype A and B strains, but it was similar among strains of the same subtype. No subtype-specific pattern was seen in proteolytic digests of monoclonal antibody-bound G protein. INTRODUCTIONFor the 3 decades since its discovery human respiratory syncytial (RS) virus has been considered to represent a single homogeneous serotype. Although cross-neutralization tests with animal hyperimmune sera demonstrated differences between isolates of the virus (Coates et al., 1963; Wulffet al., 1964;Doggett & Taylor-Robinson, 1964) no corresponding differences were observed with infant sera and they were therefore not considered to be of any relevance. With the advent of monoclonal antibodies (MAbs) the antigenic stability of RS virus could be assessed again. Studies with such reagents revealed that isolates of RS virus exhibited variations in epitope occurrence (Gimenez et al., 1984) but that these variations were more extensive than could be explained by incidental mutational changes (Anderson et al., 1985;Mufson et al., 1985). The isolates could be separated into two categories based on their characteristic reaction pattern with different MAbs. The two groups were named RS virus subtype A and B (Mufson et al., 1985). These subtypes showed different properties in at least four different structural proteins emphasizing that they had become ecologically adjusted after a period of separate evolution. Characterization of the epidemiological occurrence of the two RS virus subtypes

show abstract

Antibodies to Respiratory Syncytial Virus Polypeptides and their Significance in Human Infection

Cited by 121 publications

References 26 publications

Nucleotide Sequence of the Respiratory Syncytial Virus Phosphoprotein Gene

Nucleotide Sequence of the Respiratory Syncytial Virus Phosphoprotein Gene

Bovine respiratory syncytial virus: first serological evidence in Uruguay

Structural Differences between Subtype A and B Strains of Respiratory Syncytial Virus

Contact Info

Product

Resources

About