TAILIEUCHUNG - Báo cáo khoa học: Identification of two late acyltransferase genes responsible for lipid A biosynthesis in Moraxella catarrhalis

DNA ligases are the enzymes essential for DNA replication, repair and recombination in all organisms. The bacterial DNA ligases involved in DNA replication require NAD + for activity, but eukaryotic and viral DNA ligases require ATP. | ỊFEBS Journal Identification of two late acyltransferase genes responsible for lipid A biosynthesis in Moraxella catarrhalis Song Gao1 z Daxin Peng1 z Wenhong Zhang1 Artur Muszynski2 Russell W. Carlson2 and Xin-Xing Gu1 1 Vaccine Research Section National institute on Deafness and Other Communication Disorders Rockville MD USA 2 Complex Carbohydrate Research Center University of Georgia Athens GA USA Keywords late acyltransferase lipo-oligosaccharide IpxL IpxX Moraxella catarrhalis Correspondence . Gu National institute on Deafness and Other Communication Disorders 5 Research Court Rockville MD 20850 USA Fax 1 301 435 4040 Tel 1 301 402 2456 E-mail guxx@ Present address Schoolof Veterinary Medicine Yangzhou University Yangzhou Jiangsu 225009 China Database The nucleotide sequences of IpxXand IpxL in M. catarrhalis strain O35E have been deposited in the GenBank database under the accession numbers EU155137 and EU155138 respectively Received 13 June 2008 revised 28 July 2008 accepted 19 August 2008 doi Lipid A is a biological component of the lipo-oligosaccharide of a human pathogen Moraxella catarrhalis. No other acyltransferases except for UDP-GlcNAc acyltransferase responsible for lipid A biosynthesis in M. catarrhalis have been identified. By bioinformatics two late acyltransferase genes lpxX and lpxL responsible for lipid A biosynthesis were identified and knockout mutants of each gene in M. catarrhalis strain O35E were constructed and named O35ElpxX and O35ElpxL. Structural analysis of lipid A from the parental strain and derived mutants showed that O35ElpxX lacked two decanoic acids C10 0 whereas O35ElpxL lacked one dodecanoic lauric acid C12 0 suggesting that lpxX encoded deca-noyl transferase and lpxL encoded dodecanoyl transferase. Phenotypic analysis revealed that both mutants were similar to the parental strain in their toxicity in vitro. However O35ElpxX was sensitive to the bactericidal activity of .

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