Abstract
A previous paper described the purification of a calcium-dependent lipopolysaccharide-binding protein from the hemolymph of Periplaneta americana (Jomori, T., Kubo, T., and Natori, S. (1990) Eur. J. Biochem. 190, 201-206). This paper describes the molecular cloning and characterization of cDNA for the LPS-binding protein. This protein was found to have a carbohydrate-recognition domain at its carboxyl terminus containing amino acid sequences that are conserved in various mammalian C-type lectins. It was also shown to contain an N-linked carbohydrate chain, and the amino acid residue carrying this chain was assigned as Asn at position 56 (23rd amino acid residue from the amino terminus). Northern blot analysis revealed the presence of multiple mRNAs that hybridized with this cDNA and transient increases in their content after injection of Escherichia coli into adult Periplaneta, suggesting that the LPS-binding protein plays a role in the acute phase response of this insect.
Highlights
A previous paper described the purification ocfaal- Previously, we reported the purification of a hemolymph cium-dependenltipopolysaccharide-bindinpgrotein protein of Periplaneta americana (American cockroach) havfromthehemolymphof Periplaneta americana (Jo- ing specific affinity to Escherichia coli LPS [14]
The deduced amino acid sequence revealed that this their content after injection of Escherichia coli into protein contains a consensus sequence for carbohydrate recadult Periplaneta, suggesting thattheLPS-binding ognition domains of various mammalian C-type lectins in its protein plays a role in the acute phase respontsheisof carboxyl terminus
Analysis of the cDNA revealed that thisLPS-binding protein contains a carbohydrate-binding domain at its carboxyl terminus that is conserved in various C-type lectins [33]
Summary
From the Faculty of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113,Japan. This protein was found to haveacarbohydrate-recognitiondomainat its carboxyl terminus containing amino acid sequences that are conserved in various mammalian C-tylpeectins. Northerannabllyo-t positions of E. coli and Salmonella minnesota LPS are the same, this LPS-binding protein could not bind to the latter LPS because its alignments of the tetrasaccharides aredifferent [15,16,17] These findings suggested the presence of a family of LPS-binding proteinswith different carbohydrate specificities in the hemolymph of P. americana that respond to LPS from various bacteria. The deduced amino acid sequence revealed that this their content after injection of Escherichia coli into protein contains a consensus sequence for carbohydrate recadult Periplaneta, suggesting thattheLPS-binding ognition domains of various mammalian C-type lectins in its protein plays a role in the acute phase respontsheisof carboxyl terminus. The abbreviations used are: LPS, lipopolysaccharide; SDS, sodium dodecyl sulfate; kb, kilobase(s); bp, base pair(s)
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