1992
DOI: 10.1016/0042-6822(92)90237-j
|View full text |Cite
|
Sign up to set email alerts
|

In situ immunogold labeling analysis of the rice hoja blanca virus nucleoprotein and major noncapsid protein

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
8
0

Year Published

1993
1993
2005
2005

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 22 publications
(9 citation statements)
references
References 24 publications
1
8
0
Order By: Relevance
“…The FIs found in PPSMV-infected cells are possibly a nonstructural inclusion protein of PPSMV (30). Although tenuiviruses do not produce cellular inclusion bodies that resemble the MBBs found in PPSMV-infected cells, their nonstructural protein inclusions (NCP) in infected cells resemble the FIs of PPSMV (10,11,30). PPSMV also resembles tospoviruses, which share many properties with tenuiviruses (12).…”
Section: Discussionmentioning
confidence: 99%
“…The FIs found in PPSMV-infected cells are possibly a nonstructural inclusion protein of PPSMV (30). Although tenuiviruses do not produce cellular inclusion bodies that resemble the MBBs found in PPSMV-infected cells, their nonstructural protein inclusions (NCP) in infected cells resemble the FIs of PPSMV (10,11,30). PPSMV also resembles tospoviruses, which share many properties with tenuiviruses (12).…”
Section: Discussionmentioning
confidence: 99%
“…The putative 94K protein (pc2) carries stretches of amino acid sequence showing weak similarity to parts of the membrane glycoproteins of Punta Toro virus, Rift Valley fever virus and Uukuniemi virus, all three in the genus Phlebovirus, suggesting an evolutionary relationship between the animal phleboviruses and the plant tenuiviruses [11,18]. Thus, tenuiviruses might be expected to have the enveloped virion form of Bunyaviruses but no such form has so far been found in either infected plants or insects [19][20][21][22][23]. The analogous Phlebovirus protein is processed into two glycoproteins, G1 of 72 kDa from the N-terminal part and G2, a 67 kDa protein from the C-terminal part.…”
Section: Introductionmentioning
confidence: 95%
“…For RHBV, Morales & Niessen (1985) reported both 3 nm-and 8 nm-wide filaments that may adopt helical or loose configurations. Mostly circular RHBV RNPs, 8 nm wide and of variable lengths were also observed (Espinoza et al, 1992(Espinoza et al, , 1993. For MStV, 3 nm-wide filaments (Gingery et al, 1981), but also circular and 8 nm-wide rod-shaped forms have been described (reviewed in Gingery, 1988).…”
Section: Morphology and Structural Componentsmentioning
confidence: 99%