Single amino acid substitutions in the hemagglutinin can alter the host range and receptor binding properties of H1 strains of influenza A virus

Aytay, S.; Schulze, Irene T.

doi:10.1128/jvi.65.6.3022-3028.1991

Cited by 55 publications

(16 citation statements)

References 42 publications

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“…Similar results were obtained with another pair of H1 variants, where acquisition of a carbohydrate side chain at almost the same site caused a shift in receptor specificity from binding to ␣-2,6-linked neuraminic acid to binding to ␣-2,3linked neuraminic acid. In the latter case, the altered glycosylation pattern was also accompanied by a change in host range (1). In light of these observations, our study supports the concept that by modulating receptor specificity and receptor avidity, glycosylation near the receptor binding site may be an important determinant for cell tropism and host range.…”

Section: Discussionsupporting

confidence: 84%

Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety

Ohuchi

Feldmann

et al. 1997

J Virol

172

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The hemagglutinin (HA) of the fowl plague virus (FPV) strain of influenza A virus has two N-linked oligosaccharides attached to Asn123 and Asn149 in the vicinity of the receptor binding site. The effect of these carbohydrate side chains on the binding of HA to neuraminic acid-containing receptors has been analyzed. When the oligosaccharides were deleted by site-specific mutagenesis, HA expressed from a simian virus 40 vector showed enhanced hemadsorbing activity. Binding was so strong under these conditions that erythrocytes were no longer released by viral neuraminidase and that release was significantly reduced when neuraminidase from Vibrio cholerae was used. Similarly, when these oligosaccharides were removed selectively from purified viruses by N-glycosidase F, such virions were unable to elute from receptors, although they retained neuraminidase activity. Thus, release of FPV from cell receptors depends on the presence of the HA glycans at Asn123 and Asn149. On the other hand, receptor binding was abolished when these oligosaccharides were sialylated after expression in the absence of neuraminidase (M. Ohuchi, A. Feldmann, R. Ohuchi, and H.-D. Klenk, Virology 212:77-83, 1995). These observations indicate that the receptor affinity of FPV HA is controlled by oligosaccharides adjacent to the receptor binding site.

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Section: Discussionsupporting

confidence: 84%

Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety

Ohuchi

Feldmann

et al. 1997

J Virol

172

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“…The consistency of negative pleiotropy among the mutations in our collection contrasts with the mixed results of previous studies of host range expansion in which individual mutations were approximately equally likely to exhibit positive and negative pleiotropy (Aytay and Schulze 1991;Subbarao et al 1993;Shioda et al 1994;Couderc et al 1996;Llmas-Saiz et al 1996;Kobasa et al 1999;Hanley et al 2003). We suspect that the high frequency of negative pleiotropy among mutations that expanded host range in f6 resulted in part because the proximate mechanism underlying host range expansion was an increase in the rate of attachment to the novel host.…”

Section: Discussioncontrasting

confidence: 72%

High Frequency of Mutations That Expand the Host Range of an RNA Virus

2007

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The ability of a virus population to colonize a novel host is predicted to depend on the equilibrium frequency of potential colonists (i.e., genotypes capable of infecting the novel host) in the source population. In this study, we investigated the determinants of the equilibrium frequency of potential colonists in the RNA bacteriophage f6. We isolated 40 spontaneous mutants capable of infecting a novel Pseudomonas syringae host and sequenced their host attachment genes to identify the responsible mutations. We observed 16 different mutations in the host attachment gene and used a new statistical approach to estimate that 39 additional mutations were missed by our screen. Phenotypic and fitness assays confirmed that the proximate mechanism underlying host range expansion was an increase in the ability to attach to the novel host and that acquisition of this ability most often imposed a cost for growth rate on two standard hosts. Considered in a population genetic framework, our data suggest that host range mutations should exist in phage populations at an equilibrium frequency (3 3 10 À4) that exceeds the phage mutation rate by more than two orders of magnitude. Thus, colonization of novel hosts is unlikely to be limited by an inability to produce appropriate mutations.

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“…Consistent with this idea, laboratory experiments suggest that viruses shift hosts by experiencing an intermediate broad‐host‐range genotype, rather than instantaneously shifting from one host range to another, nonoverlapping host range. Thus, the vast majority of identified host‐range mutations are shown to expand the host breadth of a virus, instead of causing an immediate host‐shift (e.g., Zarling et al 1977; Aytay and Schulze 1991). Extensive evidence from animal, plant, and bacterial viruses shows that these broad host‐range viruses readily lose host range when allowed to adapt to a single host (e.g., reviewed in Fenner and Cairns 1959; Reddy and Black 1974; Marchette et al 1990; Wichman et al 1999; Crill et al 2000; Ebert 2000).…”

Section: Discussionmentioning

confidence: 99%

Evolution of Host Specificity Drives Reproductive Isolation Among Rna Viruses

2007

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Ecological speciation hypotheses claim that assortative mating evolves as a consequence of divergent natural selection for ecologically important traits. Reproductive isolation is expected to be particularly likely to evolve by this mechanism in species such as phytophagous insects that mate in the habitats in which they eat. We tested this expectation by monitoring the evolution of reproductive isolation in laboratory populations of an RNA virus that undergoes genetic exchange only when multiple virus genotypes coinfect the same host. We subjected four populations of the RNA bacteriophage 6 to 150 generations of natural selection on a novel host. Although there was no direct selection acting on host range in our experiment, three of the four populations lost the ability to infect one or more alternative hosts. In the most extreme case, one of the populations evolved a host range that does not contain any of the hosts infectible by the wild-type 6. Whole genome sequencing confirmed that the resulting reproductive isolation was due to a single nucleotide change, highlighting the ease with which an emerging RNA virus can decouple its evolutionary fate from that of its ancestor. Our results uniquely demonstrate the evolution of reproductive isolation in allopatric experimental populations. Furthermore, our data confirm the biological credibility of simple "no-gene" mechanisms of assortative mating, in which this trait arises as a pleiotropic effect of genes responsible for ecological adaptation.

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Single amino acid substitutions in the hemagglutinin can alter the host range and receptor binding properties of H1 strains of influenza A virus

Cited by 55 publications

References 42 publications

Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety

Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety

High Frequency of Mutations That Expand the Host Range of an RNA Virus

Evolution of Host Specificity Drives Reproductive Isolation Among Rna Viruses

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