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. 1995 Apr;69(4):2629–2632. doi: 10.1128/jvi.69.4.2629-2632.1995

Mapping the hemagglutination domain of rotaviruses.

E M Fuentes-Pananá 1, S López 1, M Gorziglia 1, C F Arias 1
PMCID: PMC188943  PMID: 7884915

Abstract

Most strains of animal rotaviruses are able to agglutinate erythrocytes, and the surface protein VP4 is the virus hemagglutinin. To map the hemagglutination domain on VP4 while preserving the conformation of the protein, we constructed full-length chimeras between the VP4 genes of hemagglutinating (YM) and nonhemagglutinating (KU) rotavirus strains. The parental and chimeric genes were expressed in insect cells, and the recombinant VP4 proteins were evaluated for their capacity to agglutinate human type O erythrocytes. Three chimeric genes, encoding amino acids 1 to 208 (QKU), 93 to 208 (QC), and 93 to 776 (QYM) of the YM VP4 protein in a KU VP4 background, were constructed. YM VP4 and chimeras QKU and QC were shown to specifically hemagglutinate, indicating that the region between amino acids 93 and 208 of YM VP4 is sufficient to determine the hemagglutination activity of the protein.

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Selected References

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  1. Bass D. M., Mackow E. R., Greenberg H. B. Identification and partial characterization of a rhesus rotavirus binding glycoprotein on murine enterocytes. Virology. 1991 Aug;183(2):602–610. doi: 10.1016/0042-6822(91)90989-o. [DOI] [PubMed] [Google Scholar]
  2. Both G. W., Bellamy A. R., Mitchell D. B. Rotavirus protein structure and function. Curr Top Microbiol Immunol. 1994;185:67–105. doi: 10.1007/978-3-642-78256-5_4. [DOI] [PubMed] [Google Scholar]
  3. Fiore L., Greenberg H. B., Mackow E. R. The VP8 fragment of VP4 is the rhesus rotavirus hemagglutinin. Virology. 1991 Apr;181(2):553–563. doi: 10.1016/0042-6822(91)90888-i. [DOI] [PubMed] [Google Scholar]
  4. Fukudome K., Yoshie O., Konno T. Comparison of human, simian, and bovine rotaviruses for requirement of sialic acid in hemagglutination and cell adsorption. Virology. 1989 Sep;172(1):196–205. doi: 10.1016/0042-6822(89)90121-9. [DOI] [PubMed] [Google Scholar]
  5. Gorziglia M., Larralde G., Kapikian A. Z., Chanock R. M. Antigenic relationships among human rotaviruses as determined by outer capsid protein VP4. Proc Natl Acad Sci U S A. 1990 Sep;87(18):7155–7159. doi: 10.1073/pnas.87.18.7155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kalica A. R., Flores J., Greenberg H. B. Identification of the rotaviral gene that codes for hemagglutination and protease-enhanced plaque formation. Virology. 1983 Feb;125(1):194–205. doi: 10.1016/0042-6822(83)90073-9. [DOI] [PubMed] [Google Scholar]
  7. Keljo D. J., Smith A. K. Characterization of binding of simian rotavirus SA-11 to cultured epithelial cells. J Pediatr Gastroenterol Nutr. 1988 Mar-Apr;7(2):249–256. doi: 10.1097/00005176-198803000-00015. [DOI] [PubMed] [Google Scholar]
  8. Liprandi F., Rodriguez I., Piña C., Larralde G., Gorziglia M. VP4 monotype specificities among porcine rotavirus strains of the same VP4 serotype. J Virol. 1991 Mar;65(3):1658–1661. doi: 10.1128/jvi.65.3.1658-1661.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lizano M., López S., Arias C. F. The amino-terminal half of rotavirus SA114fM VP4 protein contains a hemagglutination domain and primes for neutralizing antibodies to the virus. J Virol. 1991 Mar;65(3):1383–1391. doi: 10.1128/jvi.65.3.1383-1391.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. López S., López I., Romero P., Méndez E., Soberón X., Arias C. F. Rotavirus YM gene 4: analysis of its deduced amino acid sequence and prediction of the secondary structure of the VP4 protein. J Virol. 1991 Jul;65(7):3738–3745. doi: 10.1128/jvi.65.7.3738-3745.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Mackow E. R., Barnett J. W., Chan H., Greenberg H. B. The rhesus rotavirus outer capsid protein VP4 functions as a hemagglutinin and is antigenically conserved when expressed by a baculovirus recombinant. J Virol. 1989 Apr;63(4):1661–1668. doi: 10.1128/jvi.63.4.1661-1668.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Mackow E. R., Yamanaka M. Y., Dang M. N., Greenberg H. B. DNA amplification-restricted transcription-translation: rapid analysis of rhesus rotavirus neutralization sites. Proc Natl Acad Sci U S A. 1990 Jan;87(2):518–522. doi: 10.1073/pnas.87.2.518. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Méndez E., Arias C. F., López S. Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture. J Virol. 1993 Sep;67(9):5253–5259. doi: 10.1128/jvi.67.9.5253-5259.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Padilla-Noriega L., Werner-Eckert R., Mackow E. R., Gorziglia M., Larralde G., Taniguchi K., Greenberg H. B. Serologic analysis of human rotavirus serotypes P1A and P2 by using monoclonal antibodies. J Clin Microbiol. 1993 Mar;31(3):622–628. doi: 10.1128/jcm.31.3.622-628.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Preugschat F., Strauss J. H. Processing of nonstructural proteins NS4A and NS4B of dengue 2 virus in vitro and in vivo. Virology. 1991 Dec;185(2):689–697. doi: 10.1016/0042-6822(91)90540-r. [DOI] [PubMed] [Google Scholar]
  16. Ruggeri F. M., Greenberg H. B. Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture. J Virol. 1991 May;65(5):2211–2219. doi: 10.1128/jvi.65.5.2211-2219.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Shaw A. L., Rothnagel R., Chen D., Ramig R. F., Chiu W., Prasad B. V. Three-dimensional visualization of the rotavirus hemagglutinin structure. Cell. 1993 Aug 27;74(4):693–701. doi: 10.1016/0092-8674(93)90516-S. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Taniguchi K., Maloy W. L., Nishikawa K., Green K. Y., Hoshino Y., Urasawa S., Kapikian A. Z., Chanock R. M., Gorziglia M. Identification of cross-reactive and serotype 2-specific neutralization epitopes on VP3 of human rotavirus. J Virol. 1988 Jul;62(7):2421–2426. doi: 10.1128/jvi.62.7.2421-2426.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Willoughby R. E., Yolken R. H. SA11 rotavirus is specifically inhibited by an acetylated sialic acid. J Infect Dis. 1990 Jan;161(1):116–119. doi: 10.1093/infdis/161.1.116. [DOI] [PubMed] [Google Scholar]
  20. Yolken R. H., Willoughby R., Wee S. B., Miskuff R., Vonderfecht S. Sialic acid glycoproteins inhibit in vitro and in vivo replication of rotaviruses. J Clin Invest. 1987 Jan;79(1):148–154. doi: 10.1172/JCI112775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Zhou Y. J., Burns J. W., Morita Y., Tanaka T., Estes M. K. Localization of rotavirus VP4 neutralization epitopes involved in antibody-induced conformational changes of virus structure. J Virol. 1994 Jun;68(6):3955–3964. doi: 10.1128/jvi.68.6.3955-3964.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]

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