ABSTRACT
Purification of pili from different organisms has shown that in general the surface protein antigens possess a relatively high percentage of hydrophobic amino acids. Several methods have been developed to measure cell surface hydrophobicity. Suspending fimbriated bacteria in salt solutions of different ionic strength to measure binding to the Hydrophobic Interaction Chromatography gels gave a simple semiquantitative method to define bacterial cell surface hydrophobicity. Comparative studies with low molecular weight hydrophobic compounds, such as H palmitic acid or certain hydrophobic fluorescent dyes such as aniline naphthalene sulfonic acid would also be interesting to utilize. Systematic studies based upon the principle that salting out occurs at low salt concentrations of proteins with hydrophobic properties such as intrinsic membrane proteins are highly desirable. Classical studies on the pathogenesis of porcine Escherichia coli diarrhea by H. R. Smith, G. W. Jones, and J. M. Rutter showed that surface proteins are necessary to cause colonization of the small intestine.
