A serotyping scheme for Campylobacter jejuni was developed based on slide agglutination of live bacteria with whole cell antisera absorbed with homologous heated and heterologous unheated cross-reactive antigens. Among 815 isolates from human and nonhuman sources, 21 serogroups were recognized. Of the 615 isolates from human cases of gastroenteritis, 529 (86%) were typable; 455 strains agglutinated in 20 single antisera, whereas 74 isolates agglutinated in various pairs of antisera, allowing subdivision of some main serogroups into subserogroups. Of the 200 isolates of C. jejuni from nonhuman sources (chicken, swine, etc.), 166 (83%) were typable, 145 cultures agglutinated in various single antisera, and 21 strains agglutinated with different pairs of antisera. Among isolates from all sources, 8 serogroups (1, 2, 4, 5, 7, 8, 9, and 11) were encountered most frequently. Serogroups 1, 2, 4, 5, 7, 9, and 11 were most common among human isolates; the majority of the chicken and all of the swine isolates belonged to the same serogroups identified from human cases. Very good serological correlation was obtained in 20 family outbreaks and 4 community outbreaks.

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In Escherichia coli, the waaP (rfaP) gene product was recently shown to be responsible for phosphorylation of the first heptose residue of the lipopolysaccharide (LPS) inner core region. WaaP was also shown to be necessary for the formation of a stable outer membrane. These earlier studies were performed with an avirulent rough strain of E. coli (to facilitate the structural chemistry required to properly define waaP function); therefore, we undertook the creation of a waaP mutant of Salmonella enterica serovar Typhimurium to assess the contribution of WaaP and LPS core phosphorylation to the biology of an intracellular pathogen. The S. enterica waaP mutant described here is the first to be both genetically and structurally characterized, and its creation refutes an earlier claim that waaP mutations in S. enterica must be leaky to maintain viability. The mutant was shown to exhibit characteristics of the deep-rough phenotype, despite its ability to produce a full-length core capped with O antigen. Further, phosphoryl modifications in the LPS core region were shown to be required for resistance to polycationic antimicrobials. The waaP mutant was significantly more sensitive to polymyxin in both wild-type and polymyxin-resistant backgrounds, despite the decreased negative charge of the mutant LPSs. In addition, the waaP mutation was shown to cause a complete loss of virulence in mouse infection models. Taken together, these data indicate that WaaP is a potential target for the development of novel therapeutic agents.

The Gram-negative

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