CELE_T08A9.9, T08A9.9

spp-5 encodes a caenopore, a saposin (B) domain-containing protein that is a member of the saposin-like protein (SAPLIP) superfamily containing mammalian NK-lysin and granulysin and the protozoan amoebapore-like proteins; SPP-5 exhibits pore-forming activity and functions as an effector of innate immunity, demonstrating antimicrobial activity against both Gram-positive and Gram-negative bacteria; in addition, SPP-5 is also required for fully normal postembryonic growth and reproduction, likely as a result of its role in killing ingested food, such as E. coli OP50; Northern blot analysis indicates that spp-5 mRNA is expressed constitutively at high levels in the presence of OP50 and a variety of other bacteria; an SPP-5::GFP reporter fusion is expressed exclusively in the intestine; the three-dimensional solution structure of SPP-5 has been determined by NMR spectroscopy revealing five helices, connected by three disulfide bonds, arranged in a folded leaf, the characteristic signature of the SAPLIP family.

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