Pneumolysin generates multiple conductance pores in the membrane of nucleated cells.
Patch clamping was used to investigate, for the first time, the electrophysiological properties of pores formed by a cholesterol-dependent cytolysin in the membrane of nucleated cells rather than in artificial membranes as previously. Pneumolysin pores in inside-out patches of CHO cell membranes had a broad range of conductance classified into small (<200 pS), medium (>200 pS and <1 nS) and large (>1 nS). A lytic-deficient mutant of pneumolysin (W433F) induced a similar spectrum of channels but there were more small channels than with wild-type (WT) toxin and the number of events was decreased. The WT toxin also induced channels when given to the inside surface of the plasma membrane.
El-Rachkidy
Rana G
RG
Department of Infection, Immunity and Inflammation, University of Leicester, Medical Sciences Building, University Road, Leicester LE1 9HN, UK.
Davies
Noel W
NW
Andrew
Peter W
PW
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism / Q000494:pharmacology; D016466:CHO Cells; D002462:Cell Membrane / Q000187:drug effects / Q000502:physiology*; D002463:Cell Membrane Permeability / Q000187:drug effects / Q000502:physiology*; D002467:Cell Nucleus / Q000187:drug effects / Q000502:physiology; D006224:Cricetinae; D003412:Cricetulus; D004553:Electric Conductivity; D015640:Ion Channel Gating / Q000187:drug effects / Q000502:physiology*; D008564:Membrane Potentials / Q000187:drug effects / Q000502:physiology; D016062:Porosity / Q000187:drug effects; D013301:Streptolysins / Q000378:metabolism* / Q000494:pharmacology*
D001426:Bacterial Proteins; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae