Amino acids of alfalfa mosaic virus coat protein that direct formation of unusually long virus particles
V Thole, R Miglino and JF Bol Institute of Molecular Plant Sciences, Gorlaeus Laboratories, Leiden University, The Netherlands. In contrast to most alfalfa mosaic virus (AMV) strains (YSMV, S, M and 425), AMV strains VRU and 1 5/64 can form abnormally long virus particles, an ability which has been...
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Veröffentlicht in: | Journal of general virology 1998-12, Vol.79 (12), p.3139-3143 |
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Sprache: | eng |
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Zusammenfassung: | V Thole, R Miglino and JF Bol
Institute of Molecular Plant Sciences, Gorlaeus Laboratories, Leiden University, The Netherlands.
In contrast to most alfalfa mosaic virus (AMV) strains (YSMV, S, M and
425), AMV strains VRU and 1 5/64 can form abnormally long virus particles,
an ability which has been linked to the coat protein (CP). In order to
study this phenomenon, the CP-encoding RNAs 3 of AMV strains VRU and 1 5/64
were cloned and fully sequenced. Comparative sequence analyses of AMV RNA 3
sequences derived from different strains revealed two non-conservative
amino acid substitutions, Ser65 and Leu175, which occur exclusively in the
closely related VRU- and 15/64- CPs. When these amino acid alterations were
introduced into the CP of AMV strain 425 unusually long virus particles
were assembled. This confirms that amino acids Ser66 and Leu175 of the CPs
of AMV strains VRU and 15/64 are involved in the formation of tubular virus
particles. |
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ISSN: | 0022-1317 1465-2099 |
DOI: | 10.1099/0022-1317-79-12-3139 |