Abstract
When purified hemagglutinating virus of Japan (HVJ) was treated with trypsin, two major surface antigens were released from the virus. The “hemagglutinin” subunits obtained by this method were reactive with homologous hemagglutination-inhibition antibody and could be detected by an antibody-blocking test. They adsorbed to but did not agglutinate red cells and thus appeared to be “monovalent.” The neuraminidase subunits were obtained in fully active form and did not adsorb to red cells. This finding suggests that these two activities of HVJ are associated with different subunits of the virus particle. The hemagglutinin and neuraminidase subunits could be partially separated by zonal rate centrifugation or gel filtration on Sephadex G-200. The molecular weights estimated for these subunits were approximately 124,000 and 114,000, respectively. After treatment with trypsin, virus-associated hemagglutinin and neuraminidase activities were both reduced significantly. The electron micrographs of such trypsinized virus particles showed complete or partial loss of surface projections. These results suggested that the subunits obtained by this method seemed to be those projections liberated from the virus by the action of trypsin.
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- Biddle F. The action of protease on influenza A2 virus. J Gen Virol. 1968 Jan;2(1):19–28. doi: 10.1099/0022-1317-2-1-19. [DOI] [PubMed] [Google Scholar]
- Cartwright B., Smale C. J., Brown F. Surface structure of vesicular stomatitis virus. J Gen Virol. 1969 Jul;5(1):1–10. doi: 10.1099/0022-1317-5-1-1. [DOI] [PubMed] [Google Scholar]
- FRENCH E. L., ADA G. L. Stimulation of the production of neuraminidase in Vibrio cholerae cultures by N-acetylneuraminic acid and sialyl-lactose. J Gen Microbiol. 1959 Dec;21:550–560. doi: 10.1099/00221287-21-3-550. [DOI] [PubMed] [Google Scholar]
- HORNE R. W., WATERSON A. P., WILDY P., FARNHAM A. E. The structure and composition of the myxoviruses. I. Electron microscope studies of the structure of myxovirus particles by negative staining techniques. Virology. 1960 May;11:79–98. doi: 10.1016/0042-6822(60)90056-8. [DOI] [PubMed] [Google Scholar]
- Kendal A. P., Apostolov K., Belyavin G. The effect of protease treatment on the morphology of influenza A, B and C viruses. J Gen Virol. 1969 Jul;5(1):141–143. doi: 10.1099/0022-1317-5-1-141. [DOI] [PubMed] [Google Scholar]
- Laver W. G., Kilbourne E. D. Identification in a recombinant influenza virus of structural proteins derived from both parents. Virology. 1966 Nov;30(3):493–501. doi: 10.1016/0042-6822(66)90125-5. [DOI] [PubMed] [Google Scholar]
- Laver W. G., Valentine R. C. Morphology of the isolated hemagglutinin and neuraminidase subunits of influenza virus. Virology. 1969 May;38(1):105–119. doi: 10.1016/0042-6822(69)90132-9. [DOI] [PubMed] [Google Scholar]
- MAYRON L. W., ROBERT B., WINZLER R. J., RAFELSON M. E., Jr Studies on the neuraminidase of influenza virus. I. Separation and some properties of the enzyme from Asian and PR8 strains. Arch Biochem Biophys. 1961 Mar;92:475–483. doi: 10.1016/0003-9861(61)90387-3. [DOI] [PubMed] [Google Scholar]
- Maeno K., Kilbourne E. D. Developmental sequence and intracellular sites of synthesis of three structural protein antigens of influenza A2 virus. J Virol. 1970 Feb;5(2):153–164. doi: 10.1128/jvi.5.2.153-164.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NOLL H., AOYAGI T., ORLANDO J. The structural relationship of sialidase to the influenza virus surface. Virology. 1962 Sep;18:154–157. doi: 10.1016/0042-6822(62)90193-9. [DOI] [PubMed] [Google Scholar]
- Webster R. G., Darlington R. W. Disruption of myxoviruses with Tween 20 and isolation of biologically active hemagglutinin and neuraminidase subunits. J Virol. 1969 Aug;4(2):182–187. doi: 10.1128/jvi.4.2.182-187.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]

