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Literature DB >> 1589965

Amino-acid sequence comparison of nepovirus coat proteins.

H Steinkellner¹, G Himmler, R Sagl, D Mattanovich, H Katinger.

Abstract

The amino acid sequence of the coat proteins of several nepoviruses was determined by a combination of peptide and nucleic acid sequencing (grapevine fanleaf virus, arabis mosaic virus, tomato blackring virus, grapevine chrome mosaic virus). These sequences were compared and showed homologies ranging from 10% to 69%, and 96.7% for the two arabis mosaic virus strains. 10% homology does not reflect any relationship between viruses, and our results implicate, that nepoviruses, considering the homology of the coat protein sequences of viruses as a parameter for virus taxonomy, may be divided into several subgroups.

Entities: Species

Mesh：

Year: 1992 PMID： 1589965 DOI： 10.1007/bf01703068

Source DB: PubMed Journal: Virus Genes ISSN： 0920-8569 Impact factor: 2.332

14 in total

1. Nucleotide sequence of AMV-capsid protein-gene.

Authors: H Steinkellner; G Himmler; D Mattanovich; H Katinger
Journal: Nucleic Acids Res Date: 1990-12-11 Impact factor: 16.971

Review 2. Evolution of plus-strand RNA viruses.

Authors: R Goldbach; J Wellink
Journal: Intervirology Date: 1988 Impact factor: 1.763

Review 3. Structure of potyvirus coat proteins and its application in the taxonomy of the potyvirus group.

Authors: D D Shukla; C W Ward
Journal: Adv Virus Res Date: 1989 Impact factor: 9.937

Review 4. Identification and classification of potyviruses on the basis of coat protein sequence data and serology. Brief review.

Authors: D D Shukla; C W Ward
Journal: Arch Virol Date: 1989 Impact factor: 2.574

5. Analyses of the terminal sequences of West Nile virus structural proteins and of the in vitro translation of these proteins allow the proposal of a complete scheme of the proteolytic cleavages involved in their synthesis.

Authors: T Nowak; P M Färber; G Wengler; G Wengler
Journal: Virology Date: 1989-04 Impact factor: 3.616

6. Evidence that the amino acid composition of the particle proteins of plant viruses is characteristic of the virus group. II. Discriminant analysis according to structural biological and classification properties of plant viruses.

Authors: C Fauquet; J Dejardin; J C Thouvenel
Journal: Intervirology Date: 1986 Impact factor: 1.763

Amino-acid sequence comparison of nepovirus coat proteins.

1. Nucleotide sequence of AMV-capsid protein-gene.

Review 2. Evolution of plus-strand RNA viruses.

Review 3. Structure of potyvirus coat proteins and its application in the taxonomy of the potyvirus group.

Review 4. Identification and classification of potyviruses on the basis of coat protein sequence data and serology. Brief review.

5. Analyses of the terminal sequences of West Nile virus structural proteins and of the in vitro translation of these proteins allow the proposal of a complete scheme of the proteolytic cleavages involved in their synthesis.

6. Evidence that the amino acid composition of the particle proteins of plant viruses is characteristic of the virus group. II. Discriminant analysis according to structural biological and classification properties of plant viruses.

7. Optimal alignments in linear space.

8. Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution.

9. Potyviral proteins share amino acid sequence homology with picorna-, como-, and caulimoviral proteins.

10. RNA2 of grapevine fanleaf virus: sequence analysis and coat protein cistron location.

1. A multiple alignment of the capsid protein sequences of nepoviruses and comoviruses suggests a common structure.

2. Protection against virus infection in tobacco plants expressing the coat protein of grapevine fanleaf nepovirus.