Abstract
Treatment of human group O and sheep erythrocytes with receptor-destroying enzyme rendered them inagglutinable by simian rotavirus SA-11. The erythrocyte receptors were also removed by periodate oxidation and markedly reduced by incubation with a high concentration of trypsin, but they were not altered by infectivity-enhancing concentrations of trypsin, p-hydroxymercuribenzoate, or sodium sulfite (Na2SO3). Hemagglutinating activity of the virus particles was destroyed by periodate oxidation at 37 degrees C, p-hydroxymercuribenzoate, and a high concentration of trypsin and decreased by Na2SOa but was not altered by incubation with receptor-destroying enzyme, infectivity-enhancing concentrations of trypsin, or periodate oxidation at 4 degrees C. These results indicate that neuraminic acid-containing receptor substances are involved in the interaction of the virus with human and sheep erythrocytes, and suggest that SA-11-erythrocyte union involves carbohydrate on the surface of erythrocytes but not on the virion. Sensitivities of the SA-11 hemagglutinin to alcohols and repeated freeze-thaw cycles were also investigated.
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Selected References
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- Babiuk L. A., Mohammed K., Spence L., Fauvel M., Petro R. Rotavirus isolation and cultivation in the presence of trypsin. J Clin Microbiol. 1977 Dec;6(6):610–617. doi: 10.1128/jcm.6.6.610-617.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bishai F. R., Blaskovic P., Goodwin D. Physicochemical properties of Nebraska calf diarrhea virus hemagglutinin. Can J Microbiol. 1978 Nov;24(11):1425–1430. doi: 10.1139/m78-229. [DOI] [PubMed] [Google Scholar]
- Brock T. D. The purification and characterization of an intracellular sex-specific mannan protein from yeast. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1104–1112. doi: 10.1073/pnas.54.4.1104. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CECIL R., McPHEE J. R. The sulfur chemistry of proteins. Adv Protein Chem. 1959;14:255–389. doi: 10.1016/s0065-3233(08)60613-0. [DOI] [PubMed] [Google Scholar]
- CLAMP J. R., HOUGH L. THE PERIODATE OXIDATION OF AMINO ACIDS WITH REFERENCE TO STUDIES ON GLYCOPROTEINS. Biochem J. 1965 Jan;94:17–24. doi: 10.1042/bj0940017. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fauvel M., Spence L., Babiuk L. A., Petro R., Bloch S. Hemagglutination and hemagglutination-inhibition studies with a strain of Nebraska calf diarrhea virus (bovine rotavirus). Intervirology. 1978;9(2):95–105. doi: 10.1159/000148927. [DOI] [PubMed] [Google Scholar]
- GOMATOS P. J., TAMM I. Reactive sites of reovirus type 3 and their interaction with receptor substances. Virology. 1962 Jul;17:455–461. doi: 10.1016/0042-6822(62)90140-x. [DOI] [PubMed] [Google Scholar]
- Inaba Y., Sato K., Takahashi E., Kurogi H., Akashi H., Satoda K., Omori T., Matumoto M. Production of calf rotavirus hemagglutinin inhibitors in the infected cell culture fluid. Microbiol Immunol. 1978;22(10):647–649. doi: 10.1111/j.1348-0421.1978.tb00416.x. [DOI] [PubMed] [Google Scholar]
- Inaba Y., Sato K., Takahashi E., Kurogi H., Satoda K. Hemagglutination with Nebraska calf diarrhea virus. Microbiol Immunol. 1977;21(9):531–534. doi: 10.1111/j.1348-0421.1977.tb00319.x. [DOI] [PubMed] [Google Scholar]
- KILHAM L., OLIVIER L. J. A latent virus of rats isolated in tissue culture. Virology. 1959 Apr;7(4):428–437. doi: 10.1016/0042-6822(59)90071-6. [DOI] [PubMed] [Google Scholar]
- Kalica A. R., James J. D., Jr, Kapikian A. Z. Hemagglutination by simian rotavirus. J Clin Microbiol. 1978 Mar;7(3):314–315. doi: 10.1128/jcm.7.3.314-315.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Krystal G., Perrault J., Graham A. F. Evidence for a glycoprotein in reovirus. Virology. 1976 Jul 15;72(2):308–321. doi: 10.1016/0042-6822(76)90160-4. [DOI] [PubMed] [Google Scholar]
- LERNER A. M., CHERRY J. D., FINLAND M. Hemagglutination with reoviruses. Virology. 1963 Jan;19:58–65. doi: 10.1016/0042-6822(63)90024-2. [DOI] [PubMed] [Google Scholar]
- PHILIPSON L., CHOPPIN P. W. On the role of virus sulfhydryl groups in the attachment of enteroviruses to erythrocytes. J Exp Med. 1960 Sep 1;112:455–478. [PubMed] [Google Scholar]
- Ramia S., Sattar S. A. Simian rotavirus SA-11 plaque formation in the presence of trypsin. J Clin Microbiol. 1979 Nov;10(5):609–614. doi: 10.1128/jcm.10.5.609-614.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rodger S. M., Schnagl R. D., Holmes I. H. Biochemical and biophysical characteristics of diarrhea viruses of human and calf origin. J Virol. 1975 Nov;16(5):1229–1235. doi: 10.1128/jvi.16.5.1229-1235.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rodger S. M., Schnagl R. D., Holmes I. H. Further biochemical characterization, including the detection of surface glycoproteins, of human, calf, and simian rotaviruses. J Virol. 1977 Oct;24(1):91–98. doi: 10.1128/jvi.24.1.91-98.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spence L., Fauvel M., Petro R., Babiuk L. A. Comparison of rotavirus strains by hemagglutination inhibition. Can J Microbiol. 1978 Apr;24(4):353–362. doi: 10.1139/m78-059. [DOI] [PubMed] [Google Scholar]
- Spence L., Fauvel M., Petro R., Bloch S. Haemagglutinin from Rotavirus. Lancet. 1976 Nov 6;2(7993):1023–1023. doi: 10.1016/s0140-6736(76)90860-6. [DOI] [PubMed] [Google Scholar]
- Suttajit M., Winzler R. J. Effect of modification of N-acetylneuraminic acid on the binding of glycoproteins to influenza virus and on susceptibility to cleavage by neuraminidase. J Biol Chem. 1971 May 25;246(10):3398–3404. [PubMed] [Google Scholar]
- Tillotson J. R., Lerner A. M. Effect of periodate oxidation on hemagglutinating and antibody-producing capacities of certain enteroviruses and reoviruses. Proc Natl Acad Sci U S A. 1966 Oct;56(4):1143–1150. doi: 10.1073/pnas.56.4.1143. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weiner H. L., Ramig R. F., Mustoe T. A., Fields B. N. Identification of the gene coding for the hemagglutinin of reovirus. Virology. 1978 May 15;86(2):581–584. doi: 10.1016/0042-6822(78)90099-5. [DOI] [PubMed] [Google Scholar]