YIP1 family member 4 (YIPF4) is a novel cellular binding partner of the papillomavirus E5 proteins.

Abstract:

:E5 proteins are amongst the least understood of the Human Papillomavirus (HPV) encoded gene products. They are small, membrane-integrated proteins known to modulate a number of critical host pathways associated with pathogenesis including growth factor receptor signaling and immune evasion. Their role in the virus life cycle is less clear, indicating a role in the productive stages of the life cycle. However, a mechanism for this is currently lacking. Here we describe the identification of a novel binding partner of E5, YIPF4 using yeast two-hybrid analysis. YIPF4 is also a poorly characterized membrane spanning protein. Mutagenesis studies implicated the transmembrane regions of each protein as important for their interaction. Binding to YIPF4 was found for all E5 proteins tested suggesting that this interaction may mediate a conserved E5 function. In normal human keratinocytes YIPF4 expression was down-regulated upon differentiation and this reduction was partially rescued in cells harbouring HPV. Despite the conserved nature of the interaction with E5, siRNA mediated depletion of YIPF4 failed to impede two well-characterized functions of E5, namely EGFR trafficking or HLA class I presentation. Continued studies of YIPF4 are warranted to determine its role in the PV life cycle.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Müller M,Wasson CW,Bhatia R,Boxall S,Millan D,Goh GY,Haas J,Stonehouse NJ,Macdonald A

doi

10.1038/srep12523

subject

Has Abstract

pub_date

2015-08-03 00:00:00

pages

12523

issn

2045-2322

pii

srep12523

journal_volume

5

pub_type

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