SadA, a Trimeric Autotransporter from Salmonella enterica Serovar Typhimurium, Can Promote Biofilm Formation and Provides Limited Protection against Infection
Raghunathan D., Wells TJ., Morris FC., Shaw RK., Bobat S., Peters SE., Paterson GK., Jensen KT., Leyton DL., Blair JMA., Browning DF., Pravin J., Flores-Langarica A., Hitchcock JR., Moraes CTP., Piazza RMF., Maskell DJ., Webber MA., May RC., MacLennan CA., Piddock LJ., Cunningham AF., Henderson IR.
ABSTRACTSalmonella entericais a major cause of morbidity worldwide and mortality in children and immunocompromised individuals in sub-Saharan Africa. Outer membrane proteins ofSalmonellaare of significance because they are at the interface between the pathogen and the host, they can contribute to adherence, colonization, and virulence, and they are frequently targets of antibody-mediated immunity. In this study, the properties of SadA, a purported trimeric autotransporter adhesin ofSalmonella entericaserovar Typhimurium, were examined. We demonstrated that SadA is exposed on theSalmonellacell surfacein vitroandin vivoduring infection of mice. Expression of SadA resulted in cell aggregation, biofilm formation, and increased adhesion to human intestinal Caco-2 epithelial cells. Immunization of mice with folded, full-length, purified SadA elicited an IgG response which provided limited protection against bacterial challenge. When anti-SadA IgG titers were enhanced by administering alum-precipitated protein, a modest additional protection was afforded. Therefore, despite SadA having pleiotropic functions, it is not a dominant, protective antigen for antibody-mediated protection againstSalmonella.