Plant virus transmission by plasmodiophorid fungi is associated with distinctive transmembrane regions of virus-encoded proteins

Computer analysis of published sequence data has consistently identified two complementary transmembrane domains in the coat protein readthrough domains of benyviruses, furoviruses and pomoviruses and in the P2 proteins of bymoviruses. These viruses differ in genome organisation but are all transmit...

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Bibliographic Details
Published in:Archives of virology 2001-01, Vol.146 (6), p.1139-1153
Main Authors: ADAMS, M. J, ANTONIW, J. F, MULLINS, J. G. L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animal viral diseases
Animals
Benyvirus
Biological and medical sciences
Capsid - chemistry
Capsid - genetics
CP protein
Disease Vectors
Epidemiology
Fundamental and applied biological sciences. Psychology
Furovirus
Genetic Vectors
Genome, Viral
Infectious diseases
Medical sciences
Microbiology
Models, Molecular
Molecular Sequence Data
Myxomycetes - virology
Plant Diseases - virology
Plant Viruses - classification
Plant Viruses - genetics
Plant Viruses - isolation & purification
Plant Viruses - pathogenicity
Protein Structure, Tertiary
RNA Viruses - classification
RNA Viruses - genetics
RNA Viruses - isolation & purification
RNA Viruses - pathogenicity
Sequence Deletion
Viral diseases
Virology
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Summary:Computer analysis of published sequence data has consistently identified two complementary transmembrane domains in the coat protein readthrough domains of benyviruses, furoviruses and pomoviruses and in the P2 proteins of bymoviruses. These viruses differ in genome organisation but are all transmitted by plasmodiophorid fungi. The second domain is absent or disrupted in naturally-occurring deletion mutants that cannot be fungally-transmitted. In a non-transmissible substitution mutant of Beet necrotic yellow vein virus [Tamada et al. (1996) J Gen Virol 77: 1359-1367], the alignment of the helices is disrupted. From conserved patterns detected in transmembrane helix sequences and calculated relative helix tilts, structural arrangements consistent with tight packing of transmembrane helices were identified. These included ridge/groove arrangements between the two helices and strong electrostatic associations at the interfacial regions of the membrane. The data strongly suggest that these transmembrane helices facilitate the movement of virus particles across the fungal membrane.
ISSN:0304-8608
1432-8798
DOI:10.1007/s007050170111