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Heptad-repeat sequences in the glycoprotein of rhabdoviruses
Two or three regions containing three or more successive newly defined heptads of a–d hydrophobic amino acid repeats have been located in the cDNA-derived amino acid sequences of glycoprotein G of all rhabdoviruses examined (rabies, vesicular stomatitis, fish, and plant rhabdoviruses) by computer se...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Kluwer Academic Publishers
1995
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088536/ https://www.ncbi.nlm.nih.gov/pubmed/8560770 http://dx.doi.org/10.1007/BF01702591 |
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author | Morales Coll, Julio |
author_facet | Morales Coll, Julio |
author_sort | Morales Coll, Julio |
collection | PubMed |
description | Two or three regions containing three or more successive newly defined heptads of a–d hydrophobic amino acid repeats have been located in the cDNA-derived amino acid sequences of glycoprotein G of all rhabdoviruses examined (rabies, vesicular stomatitis, fish, and plant rhabdoviruses) by computer search. These new heptad-repeats differ from those previously reported in other viruses because of the presence of all the hydrophobic amino acids in positions a or d, and because they are not predicted to form coiled coils by current methods and thus they have not been detected previously in any rhabdoviruses. The two or three heptad-repeat regions were the only parts of the glycoprotein with at least three successive heptad-repeats in all the rhabdoviral sequences studied and had low sequence variability among the members of each of the rhabdoviral genus but show no sequence similarity among the different genus. All these newly detected heptad repeats were in the vicinity of some of the higher hydrophobic regions in each of the rhabdovirus genera studied and were found mostly, but not always, outside the extra amino acid sequences that occur in the longer insect or plant rhabdovirus glycoprotein G. The correspondence of position and structure of these heptad-repeats among all the rhabdoviruses suggests its participation in common function(s), most probably related to viral fusion with cellular membranes. |
format | Online Article Text |
id | pubmed-7088536 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1995 |
publisher | Kluwer Academic Publishers |
record_format | MEDLINE/PubMed |
spelling | pubmed-70885362020-03-23 Heptad-repeat sequences in the glycoprotein of rhabdoviruses Morales Coll, Julio Virus Genes Article Two or three regions containing three or more successive newly defined heptads of a–d hydrophobic amino acid repeats have been located in the cDNA-derived amino acid sequences of glycoprotein G of all rhabdoviruses examined (rabies, vesicular stomatitis, fish, and plant rhabdoviruses) by computer search. These new heptad-repeats differ from those previously reported in other viruses because of the presence of all the hydrophobic amino acids in positions a or d, and because they are not predicted to form coiled coils by current methods and thus they have not been detected previously in any rhabdoviruses. The two or three heptad-repeat regions were the only parts of the glycoprotein with at least three successive heptad-repeats in all the rhabdoviral sequences studied and had low sequence variability among the members of each of the rhabdoviral genus but show no sequence similarity among the different genus. All these newly detected heptad repeats were in the vicinity of some of the higher hydrophobic regions in each of the rhabdovirus genera studied and were found mostly, but not always, outside the extra amino acid sequences that occur in the longer insect or plant rhabdovirus glycoprotein G. The correspondence of position and structure of these heptad-repeats among all the rhabdoviruses suggests its participation in common function(s), most probably related to viral fusion with cellular membranes. Kluwer Academic Publishers 1995 /pmc/articles/PMC7088536/ /pubmed/8560770 http://dx.doi.org/10.1007/BF01702591 Text en © Kluwer Academic Publishers 1995 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Article Morales Coll, Julio Heptad-repeat sequences in the glycoprotein of rhabdoviruses |
title | Heptad-repeat sequences in the glycoprotein of rhabdoviruses |
title_full | Heptad-repeat sequences in the glycoprotein of rhabdoviruses |
title_fullStr | Heptad-repeat sequences in the glycoprotein of rhabdoviruses |
title_full_unstemmed | Heptad-repeat sequences in the glycoprotein of rhabdoviruses |
title_short | Heptad-repeat sequences in the glycoprotein of rhabdoviruses |
title_sort | heptad-repeat sequences in the glycoprotein of rhabdoviruses |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088536/ https://www.ncbi.nlm.nih.gov/pubmed/8560770 http://dx.doi.org/10.1007/BF01702591 |
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