Membrane-permeabilizing motif in Semliki forest virus E1 glycoprotein.
Cell infection by alphaviruses is accompanied by membrane permeability changes. New predictive approaches, including the computation of interfacial affinity and corresponding hydrophobic moments, suggest a segmented amphipathic-at-interface domain in the stem region of Semliki Forest virus fusion protein E1. Expression of E1 sequences in Escherichia coli cells confirmed that the membrane proximal plus transmembrane (TM) domain unit permeabilizes cells as efficiently as the 6K viroporin. Both our predictive and experimental data support the involvement of the E1 stem-TM region in membrane insertion and permeabilization. We propose to combine Wimley-White hydrophobicity analysis with expression-coupled permeability assays in order to identify viral products implied in breaching cell membrane barriers during infection.
Nieva
José L
JL
Unidad de Biofísica (CSIC-UPV/EHU), Departamento de Bioquímica, Universidad del País Vasco, Apdo., 644, 48080 Bilbao, Spain. gbphniesj@lg.ehu.es
Sanz
Miguel A
MA
Carrasco
Luis
L
D000818:Animals; D002461:Cell Line, Transformed; D002462:Cell Membrane / Q000502:physiology / Q000821:virology; D002463:Cell Membrane Permeability / Q000502:physiology*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D008562:Membrane Glycoproteins / Q000502:physiology*; D012672:Semliki forest virus / Q000502:physiology*; D014759:Viral Envelope Proteins / Q000502:physiology*
C494127:E1 glycoprotein, Semliki forest virus; D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins