HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Bosch, V. Articles by Steinhauer, D. A. Search for Related Content PubMed PubMed Citation Articles by Bosch, V. Articles by Steinhauer, D. A. Agricola Articles by Bosch, V. Articles by Steinhauer, D. A.

Inhibition of release of lentivirus particles with incorporated human influenza virus haemagglutinin by binding to sialic acid-containing cellular receptors

Forschungsschwerpunkt Angewandte Tumorvirologie, F0200, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, 69120 Heidelberg, Germany¹
Division of Virology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK²

Author for correspondence: Valerie Bosch. Fax +44 6221 424932. e-mail v.bosch{at}dkfz-heidelberg.de

Mutants of the haemagglutinin (HA) gene of human influenza virus A/Aichi/2/68 (H3N2) encoding HA proteins that are proteolytically cleaved intracellularly, defective in binding to cellular receptors or defective for acylation within the cytoplasmic C terminus have been generated. Here, the properties of these mutated HA molecules are described and their incorporation into the lipid membrane of released human immunodeficiency virus (HIV)-like particles is analysed. It is demonstrated that, when produced from cells coexpressing any of the binding-competent Aichi-HA molecules, release of HIV-like particles into the extracellular medium is reduced and the particles that are released fail to incorporate Aichi-HA. These blocks in release and incorporation, respectively, can both be overcome. The release of normal amounts of particles with incorporated HA can be achieved either by mutation of the receptor-binding site on the Aichi-HA molecule or by removal of sialic acid from surface proteins with neuraminidase. In contrast, as a result of blockage of the sialic acid-binding site by sialidated oligosaccharides on the HA itself, the HA of influenza virus A/FPV/Rostock/34 (H7N1) is efficiently incorporated into HIV-like particles. These results, namely that particle release can be inhibited by interactions between the incorporated glycoprotein and the cell surface and/or that interactions with other cellular components can be inhibitory to incorporation into retrovirus envelopes, probably reflect general principles that may hold for many viral and cellular glycoproteins.

This article has been cited by other articles:

				C. Chaipan, D. Kobasa, S. Bertram, I. Glowacka, I. Steffen, T. Solomon Tsegaye, M. Takeda, T. H. Bugge, S. Kim, Y. Park, et al. Proteolytic Activation of the 1918 Influenza Virus Hemagglutinin J. Virol., April 1, 2009; 83(7): 3200 - 3211. [Abstract] [Full Text] [PDF]

				J. Meisner, K. J. Szretter, K. C. Bradley, W. A. Langley, Z.-N. Li, B.-J. Lee, S. Thoennes, J. Martin, J. J. Skehel, R. J. Russell, et al. Infectivity Studies of Influenza Virus Hemagglutinin Receptor Binding Site Mutants in Mice J. Virol., May 15, 2008; 82(10): 5079 - 5083. [Abstract] [Full Text] [PDF]

				V. Sandrin, B. Boson, P. Salmon, W. Gay, D. Negre, R. Le Grand, D. Trono, and F.-L. Cosset Lentiviral vectors pseudotyped with a modified RD114 envelope glycoprotein show increased stability in sera and augmented transduction of primary lymphocytes and CD34+ cells derived from human and nonhuman primates Blood, July 18, 2002; 100(3): 823 - 832. [Abstract] [Full Text] [PDF]