Heterotrimeric GTP-binding proteins (G-proteins) have been shown to pl
ay an important role in cellular signalling. However, G-protein involv
ement in the intracellular spreading of bacterial pathogens is still p
oorely understood. In this study, antibodies, that recognize G-protein
alpha-subunits (anti-G(alpha)), were used to investigate the localiza
tion of G-proteins in the macrophage-like cell line P388D(1) and E. co
li, also in their L-forms, during phagocytosis. In E. coli, anti-G(alp
ha)-binding sites were detected preferably in the cell wall and septa
of the whole bacterial forms as well as in the cytoplasm of L-forms. W
estern blotting of bacterial lysates demonstrated protein bands with p
ositive immunoreaction to antibodies against G(s alpha), G(i alpha), a
nd G(common alpha) with a higher affinity to the antibody against G(s
alpha). Immunoreaction with the anti-G(s alpha)-antibody was markedly
higher in pathogenic strains of E. coli. Because of the conserved stru
cture in all GTP-binding proteins which seem to derive from a single p
rimordial protein involved in signal transduction mechanisms, it is re
asonable to assume that some anti-G(a)-positive proteins in E. coli mi
ght be related to G-proteins of higher organisms. A putative candidate
for bacterial G-proteins seems to be a 36 kDa protein. Enhancement in
G-protein immunostaining in the cytoplasm of macrophages around the i
nternalized bacteria testifies to the involvement of G-proteins in med
iation of endocytosis responses of phagocytes.