Journal
VIROLOGY
Volume 482, Issue -, Pages 208-217Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2015.03.047
Keywords
Citrus tristeza virus; Virus movement; Plant virus
Categories
Funding
- National Science Foundation [1050883]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1050883] Funding Source: National Science Foundation
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Citrus tristeza virus (CTV), the largest and most complex member of the family Closteroviridae, encodes a unique protein, p33, which shows no homology with other known proteins, however, plays an important role in virus pathogenesis. In this study, we examined some of the characteristics of p33. We show that p33 is a membrane-associated protein that is inserted into the membrane via a transmembrane helix formed by hydrophobic amino acid residues at the C-terminal end of the protein. Removal of this transmembrane domain (TMD) dramatically altered the intracellular localization of p33. Moreover, the TMD alone was sufficient to confer membrane localization of an unrelated protein. Finally, a CTV variant that produced a truncated p33 lacking the TMD was unable to infect sour orange, one of the selected virus hosts, which infection requires p33, suggesting that membrane association of p33 is important for the ability of CTV to extend its host range. (C) 2015 Elsevier Inc. All rights reserved.
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