Immunelektronenmikroskopische Untersuchungen zur serologischen Verwandtschaft des Gerstengelbmosaik-Virus (barley yellow mosaic virus) und des Milden Gerstenmosaik-Virus (barley mild mosaic virus) mit anderen gestreckten Viren

Stanarius, Andreas; Proeseler, sc. Gerhard; Richter, Steffi

doi:10.1080/03235408909438880

Cited by 11 publications

(13 citation statements)

References 5 publications

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“…Relationships between BaMMV or BaYMV and aphid-borne potyviruses are even more distant. Thus, although Stanarius et al (1989) reported that BaMMV reacted with antisera to the aphid-borne potyviruses BYMV and TuMV, it has only slight capsid protein sequence similarities (21 to 26%) with these two and other aphid-borne or mite-borne potyviruses. Likewise, the BaYMV capsid protein has only weak similarity (20 to 27~) with those of aphid-borne or mite-borne potyviruses.…”

Section: Discussionmentioning

confidence: 91%

“…lmmunoelectron microscopic tests failed to detect any serological relationship between BaMMV and BaYMV, although relationships were found between BaMMV and aphid-borne potyviruses (Stanarius et al, 1989). It is therefore of great interest to compare the capsid protein amino acid sequence similarities between BaMMV and aphid-borne potyviruses or BaYMV.…”

Section: T L E T; ~1 T ~T K P )T S S F T I O S a K ~1 V (; F I Kmentioning

confidence: 99%

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Sequence analysis of the 3'-terminal halves of RNA 1 of two strains of barley mild mosaic virus

Kashiwazaki¹,

Nomura²,

Kuroda

et al. 1992

Journal of General Virology

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DNA complementary to the Y-terminal halves of RNA 1 of two strains of barley mild mosaic virus (BaMMV) from Japan, BaMMV-Kal and BaMMV-Nal, was cloned and sequenced. The sequences start within a single long open reading frame (ORF), and are followed by 337 and 338 3' non-coding nucleotides, for BaMMV-Ka 1 and BaMMV-Nal respectively. The two strains have 88 % nucleotide identity in the ORFs and 92 % identity in the non-coding regions. The putative ORF products contain the capsid proteins at the C termini, as indicated by amino acid sequence analysis, and two putative non-structural proteins are arranged in the same manner as in RNA 1 of barley yellow mosaic virus (BaYMV). The deduced capsid proteins of BaMMV-Kal and BaMMV-Nal each contain 251 amino acids and have 94 % sequence identity, which is compatible with their close serological relationship. Most of the sequence differences between the two capsid proteins are found in the N-terminal region, and might explain their serological differences. Significant sequence similarities of the capsid proteins of the two BaMMV strains (37 and 35 % respectively) with that of BaYMV, and their marginal similarities (21 to 26 %) to the capsid proteins of aphid-borne or mite-borne potyviruses support the classification of BaMMV and BaYMV as distinct members of the same virus group, which is separate from the group(s) containing aphidborne or mite-borne potyviruses.

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Section: Discussionmentioning

confidence: 91%

Section: T L E T; ~1 T ~T K P )T S S F T I O S a K ~1 V (; F I Kmentioning

confidence: 99%

Sequence analysis of the 3'-terminal halves of RNA 1 of two strains of barley mild mosaic virus

Kashiwazaki¹,

Nomura²,

Kuroda

et al. 1992

Journal of General Virology

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“…For similar reasons, viruses transmitted by, or possibly transmitted by, mites also have restricted host ranges [65]. For similar reasons, viruses transmitted by, or possibly transmitted by, mites also have restricted host ranges [65].…”

Section: Natural Host Rangementioning

confidence: 99%

“…Antisera to dissociated coat proteins had a much broader reactivity than those prepared to intact virus particles [72,77] and antisera to coat protein prepared by different procedures often differed in specificity [46]. Hence, the conclusion that degradation of potyvirus protein takes place during purification, possibly continues during immunization, and considerable caution is needed in the interpretation of serological results [65]. Antisera from early bleedings contained more specific antibodies, whereas those from later bleedings contained increasing amounts of cross-reacting antibodies [77,80,86].…”

Section: Continuing Efforts Towards Distinctionmentioning

confidence: 99%

“…When studying serological relationships, intact virus particles behave differently from dissociated protein subunits obtained by sonication or pyrrolidine treatment [65]. Partial degradation of coat protein during purification and its effect on coat-protein size determination, amino acid composition, and serology have also been recognized as problems when studying the relationships between BYMV and a number of other potyviruses [65].…”

Section: N-terminal Part Of Coat Protein: a Breakthroughmentioning

confidence: 99%

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