Immunological Detection of 22K Protein in Sporulating Cells of Bacillus megaterium ATCC 12872

Abstract

The synthesis and deposition of 22,000-dalton (22K) spore coat protein were examined immunochemically on the sporulating cells of Bacillus megaterium ATCC 12872 using the antibody to purified 22K spore coat protein. This antibody cross-reacted with 44K and 25K proteins in immunoblot analysis of dormant spore coat proteins. Immunoblot analysis on the sporulating cells showed that 22K protein was detected from t8 in forespore coat protein fractions. Sandwich enzyme immunoassay revealed that 22K protein in the spore coat protein fraction appeared at t6 and reached a plateau at t9, and 22K protein in the mother cell cytoplasmic fraction was detected at only t7 and t8 at a very low level.

BMQ_0737 encodes a novel protein crucial to the integrity of the outermost layers ofBacillus megateriumQM B1551 spores

“…Collectively, these analyses indicate that the B. megaterium QM B1551 spore coat and exosporium are comprised and assembled from a substantially different subset of proteins to their orthologous Bacillus counterparts. Several biochemical‐led studies aimed at characterising the B. megaterium QM B1551 spore coat were published through the 1970s to early 1990s (Imagawa et al ., , ; Nishihara et al ., ; Takubo et al ., ). Unfortunately, these studies predated the availability of virtually any B. megaterium genomic information and tools for targeted genetic manipulation.…”