title: Semliki Forest virus envelope proteins function as proton channels.
abstract: It has been shown that isolated nucleocapsids of Semliki Forest virus (SFV) contract upon low pH exposure (Soederlund et al., 1972). This contraction of the nucleocapsids has been used as an indicator to demonstrate that the spike proteins of SFV can translocate protons into the interior of the virus particle upon low pH (5.8) exposure. Spikeless virus particles obtained after bromelain digestion, which were used as a control, did not translocate protons. This implies that the ectodomain of the spike plays a crucial role for the proton translocation.
authors.affiliation: Central Laboratory Blood Transfusion Service, Swiss Red Cross, Bern.
authors.forename: A
authors.initials: A
authors.lastname: Schlegel
authors.forename: A
authors.initials: A
authors.lastname: Omar
authors.forename: P
authors.initials: P
authors.lastname: Jentsch
authors.forename: A
authors.initials: A
authors.lastname: Morell
authors.forename: C
authors.initials: C
authors.lastname: Kempf
mesh_terms: D000330:Aedes; D000595:Amino Acid Sequence; D000818:Animals; D002999:Clone Cells; D006863:Hydrogen-Ion Concentration; D007473:Ion Channels / Q000378:metabolism*; D008969:Molecular Sequence Data; D011522:Protons; D012672:Semliki forest virus / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000378:metabolism*
chemical_list: D007473:Ion Channels; D011522:Protons; D014759:Viral Envelope Proteins