The type II secretion machinery allows most Gram-negative bacteria to deliv
er virulence factors into their surroundings. We report that in Erwinia chr
ysanthemi, GspE (the putative NTPase), GspF, GspL and GspM constitute a com
plex in the inner membrane that is presumably used as a platform for assemb
ling other parts of the secretion machinery. The GspE-GspF-GspL-GspM comple
x was demonstrated by two methods: (i) co-immunoprecipitation of GspE-GspF-
GspL with antibodies raised against either GspE or GspF; (ii) interactions
in the yeast two-hybrid system between GspF and GspE, GspF and GspL, GspL a
nd GspM. GspL was found to have an essential role in complex formation. We
propose a model in which the GspE-GspF-GspL-GspM proteins constitute a buil
ding block within the secretion machinery on top of which another building
block, referred to as a pseudopilus, assembles. By analogy, we predict that
a similar platform is required for the biogenesis of the type IV pilus.