Campylobacterfetus strains may be of serotype A or B, a property associated with lipopolysaccharide (LPS) structure. Wild-type C. fetus strains contain surface array proteins (S-layer proteins) that may be extracted in water and that are critical for virulence. To explore the relationship of S-layer proteins to other surface components, we reattached S-layer proteins onto S-template cells generated by spontaneous mutation or by serial extractions of S' cells with water. Crystalline surface layers have been observed as the outermost component of the bacterial cell envelopes in numerous gram-positive and gram-negative species (38) and are composed of protein subunits assembled over the cell surface into two-dimensional arrays with hexagonal (p6), square (p4), or oblique (p2) symmetry (36). For the majority of bacteria, the surface layer is formed from a single species of protein, known as a surface array protein (S-layer protein), which is acidic and generally hydrophobic (36,38). In gram-negative bacteria, the constituent subunits of most S-layers interact with each other and with the underlying outer membrane components (3,35,37,40), such as outer membrane proteins in an Acinetobacter sp. (41), lipid-lipopolysaccharide (LPS) in Spirillum serpens (11), and LPS in Aeromonas salmonicida (2, 22), and many S-layers require divalent cations for assembly (10,37,40).