Figure 1.
bah-1 worms are resistant to biofilm attachment.
(A–C) Wild-type C. elegans exposed to (A) E. coli, (B) Y. pestis, and (C) Y. pseudotuberculosis. (D–F) bah-1 worms exposed to (D) E. coli, (E) Y. pestis, and (F) Y. pseudotuberculosis.
Table 1.
Location and consequence of bah-1 mutations.
Figure 2.
Phylogenetic relationships of 61 C. elegans DUF23 proteins determined by maximum parsimony.
The bootstrap consensus tree shown is inferred from 10,000 replicates. Bootstrap values shown next to the branches were used to divide the family into three clades based on characteristic motif arrangements diagramed to the right of each clade. The DUF23 domain is shaded in light gray while conserved motifs found within each clade are distinguished by darker gray or a crosshatching pattern. The previously annotated DUF23 genes C13A2.1, C13A2.11, C13A2.2, D1014.5, K08D9.5, and T13H10.2 were eliminated from consideration because they lack the conserved cysteines and acidic amino acid motif, while C27C7.2 and ZK1025.5 were eliminated due to a high probability of being pseudogenes.
Figure 3.
CLUSTAL alignment of the DUF23 domains of BAH-1 and its closest relatives in three insect species and X. laevis.
Boxed regions are the most highly conserved within DUF23 proteins. Arrows show cysteine residues with conserved spacing. Bars designate conserved acidic motif.
Figure 4.
bah-1 expression in seam cells.
(A) Expression of promoter-GFP fusion (Experimental Methods) in L2, L4 and early adult. (B) Immunofluorescence detection of epitope-tagged BAH-1 in two representative worms.
Figure 5.
Biofilm attachment phenotypes of bah-1 null, dauer defective, and dauer constitutive mutants.
Biofilm attached after 4 hours of exposure to Y. pseudotuberculosis. Data are mean±S.D. of two independent trials, with a minimum of 82 animals from each genotype per trial.