Fimbrial adhesins that mediate attachment to host cells are produced by mos
t virulent Escherichia coil isolates, These virulence factors play an impor
tant role in the initial stages of bacterial colonization and also in deter
mination of the host and tissue specificity. Isolates belonging to serotype
O78 are known to cause a large variety of clinical syndromes in farm anima
ls and humans and have been shown to produce several types of adherence fim
briae. We studied the fimbrial adhesin from an avian septicemic E. coli iso
late of serotype O78, Analysis of the genetic organization of the fac (fimb
ria of avian E. coli) gene cluster indicates that it belongs to the S-fimbr
ial adhesin family. Seven open reading frames coding for major and minor st
ructural subunits were identified, and most of them showed a high degree of
homology to the corresponding Sfa and Foc determinants. The least-conserve
d open reading frame was facS, encoding a protein known to play an importan
t role in determining adherence specificity in other S-fimbrial gene cluste
rs.