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Biomedical subjects

M W Shaw

Publications and source records attributed to M W Shaw.

At least 55 records · Page 3Linked to original sources
PubMed1984

Studies on the synthesis of the influenza V virus NB glycoprotein.

The synthesis of the influenza B virus glycoprotein NB has been demonstrated in cells infected with four different virus strains isolated from 1940 to 1983. Time-course studies have shown that the neuraminidase protein (NA) and NB appear simultaneously in infected cells, in agreement with the previous observation that both proteins are translated from a single, bicistronic mRNA. Pulse-chase experiments indicated that the NB protein disappears from infected cells within 3 hr after synthesis. The influenza B virus nonstructural protein NS2 was also observed to disappear rapidly from infected cells, with none detected 1 hr after synthesis. Immunoprecipitation of viral proteins from infected cells using hyperimmune mouse serum has demonstrated antigenic cross-reactivity among the NB proteins of the four virus strains studied. The finding of polypeptides smaller than NB that exhibit a labeling pattern with different amino acids which is characteristic of NB and which are precipitated by the mouse antiviral serum suggests that specific cleavage products of NB may be formed in infected cells.

Animals↗
PubMed1984

A specific sub-set of host-cell mRNAs prime influenza virus mRNA synthesis.

The host-cell derived RNA primer sequences at the 5' termini of mRNAs of influenza A and B viruses, obtained from sequences of 29 cDNA clones, have been compared. This has been done for clones of five different genome segments from four strains of influenza A and B virus. The results indicate that host RNA primers containing a 3'-terminal Py-G-C-A sequence before the presumed endonuclease cleavage site are preferred for use as primers in influenza virus mRNA synthesis. Primer-extension analyses of the 5'-terminal heterogeneous sequences of in vivo synthesized mRNAs confirm the preference for G-C-A-terminated primer fragments, with some differences noted between the transcripts of types A and B influenza virus genome segments.

Base Sequence↗
PubMed1983

A previously unrecognized influenza B virus glycoprotein from a bicistronic mRNA that also encodes the viral neuraminidase.

RNA segment 6 of the influenza B virus genome codes for a previously unidentified polypeptide designated NB. The reading frame for this polypeptide begins with the first AUG codon on the mRNA and overlaps the reading frame for the viral neuraminidase by 292 nucleotides. The amino acid sequence of polypeptide NB deduced from the nucleotide sequence of the B/Lee/40 strain consists of 100 amino acids with a molecular weight of 11,242. The sequence contains four potential glycosylation sites, and the protein has been found to be glycosylated in infected cells. NB has not been found in virions. Sucrose gradient sedimentation and analysis of the structure of the mRNA by nuclease S1 mapping and sequence analysis by the primer extension method indicated that polypeptide NB and the neuraminidase are translated from a single bicistronic mRNA. A protein analogous to NB has not been found with influenza A virus, and this represents a major difference between the two virus types.

Amino Acid Sequence↗
PubMed1982

Immunologic studies on the influenza A virus nonstructural protein NS1.

We purified the major influenza virus nonstructural protein, designated NS1, from cytoplasmic inclusions that were solubilized and used to raise antisera in rabbits. One of the antisera was found to be specific for NS1 by complement fixation tests and analyses of immune precipitates. Antiserum to NS1 isolated from cells infected with A/WSN/33 virus specifically precipitated NS1 from extracts of cells infected with seven distinct isolates of influenza A virus representing five different antigenic subtypes. These included A/WSN/33, A/PR/8/34, A/FW/5/50, A/USSR/90/77, A/RI/5+/57, A/Victoria/3/75, and A/Swine /1977/31; however, NS1 from cells infected with B/Lee/40 virus was not precipitated. Radioimmunoassays using radioiodinated NS1 protein from A/WSN virus-infected cells and unlabeled cytoplasmic extracts of cells infected with various strains of influenza virus as competitors indicated significant antigenic cross-reactivities for the NS1 proteins of all influenza A viruses tested. The results suggest a gradual antigenic drift over the 45 yr separating the earliest and most recent virus isolates examined. Thus, compared with the virion neuraminidase and hemagglutinin antigens, NS1 appears to be highly conserved in different influenza A virus isolates.

Animals↗
PubMed1982

Complete nucleotide sequence of the neuraminidase gene of influenza B virus.

The complete nucleotide sequence of the neuraminidase gene of influenza virus B/Lee/40 was derived from a cloned cDNA copy of virion RNA segment 6 and its corresponding mRNA. The RNA segment contains 1,557 virus-specific nucleotides, and the protein encoded by the longest open reading frame has a total of 466 amino acids with a molecular weight of 51,721. As is the case with the influenza A virus neuraminidases, the deduced amino acid sequence of the influenza B protein includes a single hydrophobic region near the amino terminus which would be capable of spanning the lipid bilayer of the viral or cell membrane. There are four potential glycosylation sites in the protein, two of which are near the amino-terminal hydrophobic region. Comparisons of the nucleotide and amino acid sequences with those of influenza A virus neuraminidases revealed seven regions of extensive homology within the central portion of the molecules, including 12 conserved cysteine residues. Five other cysteine residues in the terminal portions were also conserved.

Base Sequence↗
PubMed1981

Surface expression of a nonstructural antigen on influenza A virus-infected cells.

Rabbit antiserum to the influenza A virus nonstructural protein, NS1, was used for indirect immunofluorescence studies of infected cells. Nonstructural antigens were detected on surfaces of P815 cells as early as 4 h after infection with A/WSN/40 virus. Adsorption of the serum with virion structural proteins did not affect the observed fluorescence, and a progressive increase in surface fluorescence at later times postinfection indicated that the surface antigen was newly synthesized during the replication cycle.

Animals↗
PubMed1981

Antibody-dependent cell-mediated cytotoxicity by human lymphocytes. II. Comparison with polymorphonuclear leukocytes against erythrocyte and nucleated target cells.

Human peripheral blood lymphocytes were compared to neutrophils with respect to their cytotoxic activity against IgG-sensitized erythrocytes (ox; ORBC) and nucleated (Raji) target cells in vitro. Overall, neutrophils were more efficient than lymphocytes in lysing erythrocytes, but lymphocytes were more efficient in lysing Raji cells. The antibody concentrations producing maximal levels of lysis against erythrocyte target cells were similar for both kinds of effector cells and guinea pig complement; however, in order to obtain Raji cell lysis mediated by neutrophils at a level comparable to that produced by lymphocytes a higher concentration of antibody was required. Another difference found between the lytic activity of these effector cell populations was kinetics of lysis against erythrocyte target: a 15 min lag phase was consistently observed only with neutrophil effector cells. Both effector cells lyse Raji cells with similar kinetics and no lag phase. Lysis by lymphocytes and neutrophils was directly proportional to the effector:target cell (E:T) ratio against both target cells. The effector cells were similarly inhibited from lysis of erythrocytes by IgG aggregate, but neutrophil lysis of Raji cells appeared to be more sensitive to inhibition. The neutrophils did not lyse nonsensitized bystander cells, and lymphocytes lysed sheep erythrocyte bystander cells only.

Antibody-Dependent Cell Cytotoxicity↗
PubMed1980

Sodium azide inhibition of complement-mediated functions.

Moderate concentrations of sodium azide (0.1-0.2%) significantly inhibited guinea-pig and human complement-mediated lysis of both IgM- and IgG-sensitized sheep erythrocytes. The reduction in cytolysis was not attributable to non-specific ionic effects, to inactivation of native complement components by azide, or to irreversible interactions of azide with sensitized erythrocytes. Mouse complement-dependent opsonization of sensitized erythrocytes, as judged by macrophage complement receptor-mediated attachment and phagocytosis of the erythrocytes, was comparably inhibited by sodium azide, suggesting that azide acted within the sequence of the first four components of the classical complement pathway.

Animals↗