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

Bosch, Valerie; Kramer, Beatrice; Pfeiffer, Tanya; Stärck, Lilian; Steinhauer, David A.

doi:10.1099/0022-1317-82-10-2485

Cited by 13 publications

(12 citation statements)

References 35 publications

(58 reference statements)

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“…FPV HA was chosen because of previous studies showing its utility in pseudotyping retrovirus vectors. [12][13][14] Specifically, we determined the effects of other influenza virus membrane proteins on the efficiency of HA pseudotyping. FPV, like other influenza A viruses, encodes three envelope proteins whose roles in virus replication have been well characterized.…”

Section: Introductionmentioning

confidence: 99%

Influenza M2 envelope protein augments avian influenza hemagglutinin pseudotyping of lentiviral vectors

et al. 2006

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Section: Introductionmentioning

confidence: 99%

Influenza M2 envelope protein augments avian influenza hemagglutinin pseudotyping of lentiviral vectors

et al. 2006

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“…This was most likely induced by neuraminidasemediated release of virions from the cell surface on which they were retained because of binding to sialic acid-containing cell surface molecules. 39,40 However, such a defect in virion egress could not explain the lack of infectivity of SIV vectors generated with the GALV and RD114 GPs because the titers of MLV vectors pseudotyped with the latter GPs are generally high. 20,33 This suggested, rather, a defect at the level of GP incorporation on the lentiviral cores.…”

mentioning

confidence: 99%

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

Sandrin

Boson

Salmon

et al. 2002

Blood

275

276

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IntroductionVectors derived from retroviruses offer particularly flexible properties in gene transfer applications given the numerous possible associations of various viral surface glycoproteins (GPs; determining cell tropism) with different types of viral cores (determining genome replication and integration). 1 For example, association of the vesicular stomatitis virus G (VSV-G) GP with viral cores derived from lentiviruses results in vector pseudotypes that have broad tropism and can integrate into nonproliferating target cells. 2 They have proved useful for the transduction of several cell types ex vivo and in vivo. [3][4][5][6][7] Yet there is considerable interest in exploring the properties of lentiviral vectors pseudotyped with alternative viral GPs. [8][9][10][11][12][13][14] This parameter is likely to modulate the physicochemical properties of the vectors, their interaction with the host immune system, and their host range. Several studies have indeed shown that the transduction efficiency of target cells is dependent on the type of GP used to coat retroviral vectors. [15][16][17][18][19][20] Additionally, some in vivo gene transfer applications will require vectors that are targeted for specific cell entry or gene expression (or both) after systemic administration. 21 Due to the wide distribution of its receptor, a lipid component of the plasma membrane, 22 VSV-G pseudotypes may bind to the surface of all cells encountered after inoculation before reaching the target cells. Moreover, VSV-Gpseudotyped vectors are rapidly inactivated by human serum 23 and this might impose a limitation on the use of VSV-G as a GP to pseudotype vectors for systemic gene delivery.Lentiviral vectors derived from simian immunodeficiency virus (SIV) have been generated in several laboratories, 1 including our own. 24 Characterization of these vectors has indicated that they are similar to those derived from human immunodeficiency virus 1 (HIV-1) with respect to the insertion of transgenes in nonproliferating cells, although SIV vectors perform better than HIV-1 vectors in simian cells. 24 Here, we report the properties of SIVmac-derived vectors pseudotyped with a panel of GPs derived from different membrane-enveloped viruses. In particular, we examined stability in human or macaque sera and gene transfer in primary hematopoietic cells including peripheral blood lymphocytes (PBLs) and CD34 ϩ cells. Materials and methods CellsThe 293T human embryo kidney cell line (American Type Culture Collection, Rockville, MD, CRL-1573) and the TE671 human rhabdomyosarcoma cell line (ATCC CRL-8805) were grown in Dulbecco modified Eagle medium (DMEM; Life Technologies, Cergy-Pontoise, France) supplemented with 10% fetal calf serum (FCS).Human and cynomolgus macaque (Macaca fascicularis) CD34 ϩ cells were obtained according to the institutional guidelines of the ethic commission from mobilized blood and bone marrow samples, respectively, as described previously. 25-27 CD34 ϩ cells were recovered after Ficoll-Paque (Amersham-Pharmacia Biot...

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“…However, since receptor binding is not required for fusion (1), such mutants may be useful as surrogate fusogenic proteins in viral vectors designed for gene therapy or targeted delivery purposes. The findings and conclusions in this report are those of the author(s) and do not necessarily represent the views of the funding agency.…”

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confidence: 99%

Infectivity Studies of Influenza Virus Hemagglutinin Receptor Binding Site Mutants in Mice

Meisner

Szretter

Bradley

et al. 2008

J Virol

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The replicative properties of influenza virus hemagglutinin (HA) mutants with altered receptor binding characteristics were analyzed following intranasal inoculation of mice. Among the mutants examined was a virus containing a Y98F substitution at a conserved position in the receptor binding site that leads to a 20-fold reduction in binding. This mutant can replicate as well as wild-type (WT) virus in MDCK cells and in embryonated chicken eggs but is highly attenuated in mice, exhibiting titers in lungs more than 1,000-fold lower than those of the WT. The capacity of the Y98F mutant to induce antibody responses and the structural locations of HA reversion mutations are examined.Influenza A viruses attach to host cells due to interactions between the hemagglutinin (HA) and cell surface glycoconjugates containing terminal sialic acids (17). A shallow depression of conserved amino acids at the membrane-distal tip of each monomer of the HA trimer serves as the receptor binding site, and this has been characterized in detail based on the structures of HA-receptor analog complexes (9,11,30,32). In all HA-receptor complexes, the location of sialic acid in the binding site is virtually superimposable in the binding pocket, while the structural configuration of the other sugars of receptor analogs can vary considerably.The type of linkage by which sialic acid is attached to the penultimate galactose sugar of influenza virus receptors can be associated with species specificity, with avian viruses preferring ␣2,3-linked receptors and human viruses favoring receptors containing ␣2,6 linkages (5, 27, 29). Numerous reports have related changes in linkage specificity to HA residues 226 and 228 (H3 numbering) at the left side of the binding site (5,14,23,28,29,(34)(35)(36)(37)39). However, studies on HA mutations associated with growth of human clinical isolates in eggs (7,8,16,24,25), variability among viruses isolated from different species (5,19,21,22,26,28), and mutations of avian virus HAs that affect the binding specificity (20,31,34,35,39,40) demonstrate that a range of residues in the vicinity of the binding site may affect receptor recognition properties. Depending on the host cells and replication environment, as well as the virus strain or subtype, any number of these residues could be relevant for adaptation.The structure of the HA of A/Aichi/2/68 virus (H3 subtype) and that of its receptor binding region are shown in Fig. 1. In a previous study, several HA mutants with substitutions at conserved positions were analyzed quantitatively for binding to human erythrocytes and a range of phenotypes was detected (18). Despite the abundance of data on receptor binding mutants, receptor specificity, and the relationship to host species for influenza viruses, there is little information that directly relates receptor binding activity that has been quantitatively determined to efficiency of influenza virus infection in vivo. Here we investigate a selection of the mutant viruses generated by reverse genetics for their ability ...

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

Abstract: Mutants of the haemagglutinin (HA) gene of human influenza virus

Cited by 13 publications

References 35 publications

Influenza M2 envelope protein augments avian influenza hemagglutinin pseudotyping of lentiviral vectors

Influenza M2 envelope protein augments avian influenza hemagglutinin pseudotyping of lentiviral vectors

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

Infectivity Studies of Influenza Virus Hemagglutinin Receptor Binding Site Mutants in Mice

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