Author: Jemielity, Stephanie; Wang, Jinyize J.; Chan, Ying Kai; Ahmed, Asim A.; Li, Wenhui; Monahan, Sheena; Bu, Xia; Farzan, Michael; Freeman, Gordon J.; Umetsu, Dale T.; DeKruyff, Rosemarie H.; Choe, Hyeryun
Title: TIM-family Proteins Promote Infection of Multiple Enveloped Viruses through Virion-associated Phosphatidylserine Document date: 2013_3_28
ID: 0fais1pz_47
Snippet: Our results, summarized in Figure 9 , demonstrate that hTIM1 is an efficient attachment factor for a range of enveloped viruses, and imply that hTIM1 promotes infection by associating with PS on the virions. PS dependency of TIM1 is supported by several independent lines of evidence. First, all pseudoviruses capable of using hTIM1 can also be enhanced by at least one other PS receptor, e.g., hTIM4 or hAxl (Fig. 7) . Second, a functional, hTIM1 PS.....
Document: Our results, summarized in Figure 9 , demonstrate that hTIM1 is an efficient attachment factor for a range of enveloped viruses, and imply that hTIM1 promotes infection by associating with PS on the virions. PS dependency of TIM1 is supported by several independent lines of evidence. First, all pseudoviruses capable of using hTIM1 can also be enhanced by at least one other PS receptor, e.g., hTIM4 or hAxl (Fig. 7) . Second, a functional, hTIM1 PS-binding domain was an absolute prerequisite for viral hTIM1 usage (Fig. 3) . Finally, the interaction between hTIM1 and GP-free virions was sufficient to elicit attachment and internalization, and this internalization was blocked by PS-containing liposomes (Figs. 4 and 5) .
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