SRA

The microbial cell surface is a critical site of microbe-host interactions that often control infection outcomes. Defining the set of host proteins present at this interface has been challenging. Here, we used a surface biotinylation approach coupled to quantitative mass spectrometry to identify and quantify both bacterial and host proteins present on the surface of diarrheal fluid-derived V. cholerae in an infant rabbit model of cholera. Our data showed that V. cholerae surfaces were coated with numerous host proteins, whose abundance were driven by the presence of cholera toxin, including the C type lectin SP-D. Mice lacking SP-D had enhanced V. cholerae intestinal colonization. Additional host proteins (AnxA1, LPO and ZAG) capable of binding V. cholerae were also found to recognize distinct taxa of the murine intestinal microbiota, suggesting that these host factors may play roles in intestinal homeostasis in addition to host defense. Proteomic analysis of microbial surfaces is valuable for identifying host interactions that regulate infection and homeostasis with both pathogens and endogenous microbiota alike. Overall design: We performed RNAseq on V. cholerae in vitro in presence of SP-D or denatured SP-D.