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2013 ; 9
(3
): e1003232
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TIM-family proteins promote infection of multiple enveloped viruses through
virion-associated phosphatidylserine
#MMPMID23555248
Jemielity S
; Wang JJ
; Chan YK
; Ahmed AA
; Li W
; Monahan S
; Bu X
; Farzan M
; Freeman GJ
; Umetsu DT
; Dekruyff RH
; Choe H
PLoS Pathog
2013[Mar]; 9
(3
): e1003232
PMID23555248
show ga
Human T-cell Immunoglobulin and Mucin-domain containing proteins (TIM1, 3, and 4)
specifically bind phosphatidylserine (PS). TIM1 has been proposed to serve as a
cellular receptor for hepatitis A virus and Ebola virus and as an entry factor
for dengue virus. Here we show that TIM1 promotes infection of retroviruses and
virus-like particles (VLPs) pseudotyped with a range of viral entry proteins, in
particular those from the filovirus, flavivirus, New World arenavirus and
alphavirus families. TIM1 also robustly enhanced the infection of
replication-competent viruses from the same families, including dengue, Tacaribe,
Sindbis and Ross River viruses. All interactions between TIM1 and pseudoviruses
or VLPs were PS-mediated, as demonstrated with liposome blocking and TIM1
mutagenesis experiments. In addition, other PS-binding proteins, such as Axl and
TIM4, promoted infection similarly to TIM1. Finally, the blocking of PS receptors
on macrophages inhibited the entry of Ebola VLPs, suggesting that PS receptors
can contribute to infection in physiologically relevant cells. Notably, infection
mediated by the entry proteins of Lassa fever virus, influenza A virus and SARS
coronavirus was largely unaffected by TIM1 expression. Taken together our data
show that TIM1 and related PS-binding proteins promote infection of diverse
families of enveloped viruses, and may therefore be useful targets for
broad-spectrum antiviral therapies.
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