1 Department of Microbiology, University of Alabama Medical Center, Birmingham, Alabama 35294
2 Institut für Medizinische Mikrobiologie der Technischen, Universität München, Munich, West Germany
ABSTRACT
The carbohydrate components of influenza C virions grown in chicken kidney (CK) cells were analyzed by gel filtration following exhaustive digestion with Pronase. The [3H]glucosamine-labeled glycopeptides were larger and more heterogeneous than those of influenza A/WSN virions; three major size classes (G1, G2, and G3) were resolved. Treatment with Vibrio cholerae neuraminidase caused a decrease in size of G1 and G2, along with release of about 16% of the 3H label. The released sugar components were identified as N-acetylneuraminic acid by thin-layer chromatography. Peak G3 was highly labeled with [3H]mannose, whereas G1 and G2 contained lower levels of mannose. The three major viral glycoproteins gp88, gp65, and gp30 were isolated from sodium dodecyl sulfate-polyacrylamide gels, and their glycopeptide components were analyzed after Pronase digestion. The three size classes of glycopeptides were obtained from any of the three glycoproteins; however, the relative amounts of the three components varied among the glycoproteins. Host cell-derived components, which appear to be mucopolysaccharides and glycoproteins, were found associated with influenza C virions grown in CK cells. These components contained glycopeptides that were mainly of sizes similar to peak G2 from influenza C virions. Previous studies have shown that influenza A/WSN virus grown in several cell types contained only two size classes of glycopeptides. Two size classes comparable to peaks G2 and G3 from influenza C virions were also observed in influenza A/WSN grown in CK cells. Thus the large G1 glycopeptides appear to be characteristic of influenza C virions.
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
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| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
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