The Cloning and Analysis of a Partial Lipase Gene Sequence of Staphylococcus hominis GIMT1.079: Partial Lipase Gene Sequencing of S. hominis

Abstract

Lipase activity is common in staphylococci. Based on the blast of various known staphylococcal lipase DNA sequences, the degenerate primers were derived to amplify a 782-bp consensus lipase gene sequence of Staphylococcus hominis GIMT1.079, which encoded a deduced polypeptide of 260 amino acid (aa) residues. The alignment of aa sequence revealed that this 260-aa partial lipase of S. hominis shared high homology with those conserved parts of other 11 deduced staphylococcal lipases, in the range of the lowest 43.0% of S. epidermidis and the highest 63.5% of S. saprophyticus. Two aa residues, Ser 39 and Asp 230 , were preliminarily confirmed in the putative catalytic triad as well as the 'P-loop' motif (-[AG]-x4-G-K-[ST]-) in this deduced 260-aa partial S. hominis lipase sequence.

Notice of Retraction: Cloning and homologous analysis of a partial lipase gene in Staphylococcus caprae TCCC 11546: Partial lipase gene sequencing of S. caprae

“…All the DNA and amino acid sequences here were analyzed using DNAMAN software (Lynnon Corp., Canada). For the convenient alignment of the amino acid sequences, the abbreviations were applied for the consensus lipase stretches from the selected strains with GenBank accession numbers in the blankets behind: S. aureus NCTC 8325, SAL (NC_007795); S. capitis SK14, SCaL-1 (EEE49083); S. caprae TCCC 11546, SCpL (GU451683); S. carnosus TM300, SCnL (AM295250); S. epidermidis ATCC 12228, SEL-1 (NP_763800); S. epidermidis M23864:W1, SEL-2 (EES41415); S. haemolyticus L62, SHaL (AF096928); S. hominis GIMT1.079, SHoL (GU111713) [10]; S. hyicus, SHyL (X02844); S. saprophyticus 7108, SSL (AY551101); S. warneri, SWL (AF208033) and S. xylosus DSM 20266, SXL (AF208229).…”

“…Since the year 1985 when Goetz et al [4] reported the first nucleotide sequence of a Staphylococus hyicus (phospho)lipase, till now at least 16 distinct lipase genes from 12 different staphylococcal species have been published, the biochemical properties of some lipases were also investigated [5][6][7][8][9][10]. In general, all these deduced staphylococcal lipases are organized as pre-pro-proteins in cytoplasm, then secreted into the culture media in pro-lipase forms, and finally processed as mature forms by the host extracellular proteases.…”

A new lipase as a pharmaceutical target for battling infections caused by Staphylococcus aureus: Gene cloning and biochemical characterization

“…The liberated free fatty acids function as nutrients for the persistence of colonized bacteria. The free fatty acids (the end products of lipolytic activity) are known to harm several immune system functions, thus might have an indirect influence on their pathogenic potential [4,15,36,37]. The most important aspect of the secreted lipases that took part in pathogenesis is the discovery of antilipase IgG antibodies in patients experiencing infections by S. aureus, enriching the virulent potential of extracellular lipases [38,39].…”