| Records |
Author  |
Cilnis, M.J.; Kang, W.; Weaver, S.C. |
| Title |
Genetic conservation of Highlands J viruses |
Type |
Journal Article |
| Year |
1996 |
Publication |
Virology |
Abbreviated Journal |
Virology |
| Volume |
218 |
Issue |
2 |
Pages |
343-351 |
| Keywords |
Alphavirus/*genetics; Alphavirus Infections/transmission/veterinary/virology; Amino Acid Sequence; Animals; Base Sequence; Conserved Sequence; Disease Outbreaks; Encephalitis, Viral/veterinary/virology; *Evolution, Molecular; Horses; Molecular Sequence Data; Phylogeny; RNA, Viral/genetics; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology, Nucleic Acid; Turkeys; Variation (Genetics)/*genetics |
| Abstract |
We studied molecular evolution of the mosquito-borne alphavirus Highlands J (HJ) virus by sequencing PCR products generated from 19 strains isolated between 1952 and 1994. Sequences of 1200 nucleotides including portions of the E1 gene and the 3' untranslated region revealed a relatively slow evolutionary rate estimated at 0.9-1.6 x 10(-4) substitutions per nucleotide per year. Phylogenetic trees indicated that all HJ viruses descended from a common ancestor and suggested the presence of one dominant lineage in North America. However, two or more minor lineages probably circulated simultaneously for periods of years to a few decades. Strains isolated from a horse suffering encephalitis, and implicated in a recent turkey outbreak, were not phylogenetically distinct from strains isolated in other locations during the same time periods. Our findings are remarkably similar to those we obtained previously for another North American alphavirus, eastern equine encephalomyelitis virus, with which Highlands J shares primary mosquito and avian hosts, geographical distribution, and ecology. These results support the hypotheses that the duration of the transmission season affects arboviral evolutionary rates and vertebrate host mobility influences genetic diversity. |
| Address |
Department of Biology, University of California, San Diego, La Jolla 92093-0116, USA |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0042-6822 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:8610461 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2657 |
| Permanent link to this record |
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| Author |
Connor, R.J.; Kawaoka, Y.; Webster, R.G.; Paulson, J.C. |
| Title |
Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates |
Type |
Journal Article |
| Year |
1994 |
Publication |
Virology |
Abbreviated Journal |
Virology |
| Volume |
205 |
Issue |
1 |
Pages |
17-23 |
| Keywords |
Amino Acid Sequence; Amino Acids/genetics; Animals; Carbohydrate Sequence; Chick Embryo; Hemagglutinin Glycoproteins, Influenza Virus; Hemagglutinins, Viral/genetics; Influenza A virus/*metabolism; Molecular Sequence Data; Receptors, Virus/*metabolism; Species Specificity; Viral Envelope Proteins/genetics |
| Abstract |
The receptor specificity of 56 H2 and H3 influenza virus isolates from various animal species has been determined to test the relevance of receptor specificity to the ecology of influenza virus. The results show that the receptor specificity of both H2 and H3 isolates evaluated for sialic acid linkage specificity and inhibition of hemagglutination by horse serum correlates with the species of origin, as postulated earlier for H3 strains based on a limited survey of five human, three avian, and one equine strain. Elucidation of the amino acid sequence of several human H2 receptor variants and analysis of known sequences of H2 and H3 isolates revealed that receptor specificity varies in association with an amino acid change at residues 228 in addition to the change at residue 226 previously documented to affect receptor specificity of H3 but not H1 isolates. Residues 226 and 228 are leucine and serine in human isolates, which preferentially bind sialic acid alpha 2,6-galactose beta 1,4-N-acetyl glucosamine (SA alpha 2,6Gal), and glutamine and glycine in avian and equine isolates, which exhibit specificity for sialic acid alpha-2,3-galactose beta-1,3-N-acetyl galactosamine (SA alpha 2,3Gal). The results demonstrate that the correlation of receptor specificity and species of origin is maintained across both H2 and H3 influenza virus serotypes and provide compelling evidence that influenza virus hosts exert selective pressure to maintain the receptor specificity characteristics of strains isolated from that species. |
| Address |
Department of Biological Chemistry, UCLA School of Medicine 90024-1737 |
| Corporate Author |
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Thesis |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0042-6822 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:7975212 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2662 |
| Permanent link to this record |
