Spirochaetal lipoproteins and pathogenesis

Haake, David A.

doi:10.1099/00221287-146-7-1491

Cited by 199 publications

(226 citation statements)

References 108 publications

(35 reference statements)

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“…Indeed, putative Lpps may represent at least 0n5-8n0 % of the bacterial proteome (Chambaud et al, 1999 ;Tjalsma et al, 1999a ;Haake, 2000). However, it remains possible that a significant proportion of these putative Lpps are ' false-positives ', misidentified due to the coincident presence of a cysteine within the signal sequences of exported proteins or proteins targeted for insertion into plasma membranes.…”

Section: Introductionmentioning

confidence: 99%

Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes

2002

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INTRODUCTIONThe bacterial cell envelope is of major significance as the focal point for interaction between the bacterium and its environment, notably the host in the case of bacterial pathogens. Bacterial cell envelope proteins thus carry out numerous important functions including roles in adhesion, nutrient acquisition and a variety of interactions with host defences. In Gram-positive bacteria the matrix of peptidoglycan and other wall polymers surrounding the cell is not an efficient barrier to the passage of small macromolecules, due both to its inherent structural permeability and to its turnover during normal cell growth. Indeed, peptidoglycan may be sufficiently permeable as to allow the passage of globular proteins of up to "50 kDa in size (Demchick & Koch, 1996 ;Dijkstra & Keck, 1996). Consequently, in the absence of a retentive outer membrane, Grampositive bacteria have evolved distinct mechanisms for retaining proteins within their cell envelopes, including covalent linkage to the peptidoglycan and non-covalent binding to teichoic acids and other cell envelope polymers (Navarre & Schneewind, 1999 ;Cossart & Jonquieres, 2000 ;Janulczyk & Rasmussen, 2001). Also significant among these mechanisms is membraneanchoring of bacterial lipoproteins (Lpps) by covalent N-terminal lipidation (Braun & Wu, 1994 ; Sutcliffe & Russell, 1995). Lpps in Gram-positive bacteria perform important roles as substrate-binding proteins (SBPs) in ABC transporter systems ; in antibiotic resistance ; in cell signalling ; in protein export and folding ; in sporulation and germination ; in conjugation and various other functions (Sutcliffe & Russell, 1995 valent to those carried out by periplasmic proteins of Gram-negative bacteria.The archetypal bacterial Lpp is the murein lipoprotein of Escherichia coli characterized by Braun and coworkers (reviewed in Braun & Wu, 1994). Structural studies revealed that a diacylglycerol moiety is thioether linked to an N-terminal cysteine of this Lpp and that this lipid group serves to orientate the protein by anchoring it to the inner leaflet of the outer membrane. Chemically identical lipid modifications have since been proposed, primarily on the basis of protein sequence analysis (see below), for a great many proteins in both Gram-positive and Gram-negative bacteria, although relatively few have received extensive biochemical characterization.Biosynthesis of bacterial lipoprotein of the ' Braun ' type proceeds via a well conserved pathway that is apparently unique to prokaryotes (Fig. 1). Following signal-peptidedirected export of the prolipoprotein (proLpp), the enzyme prolipoprotein diacylglycerol transferase (Lgt) uses phospholipid substrates and catalyses the addition of a diacylglycerol lipid unit onto the thiol of a crucial conserved cysteine which is located within a ' lipobox ' motif at the cleavage region of the proLpp signal peptide (Sankaran et al., 1995 ; Qi et al., 1995). Subsequently, the signal peptide is removed by a specific lipoprotein signal peptidase II (Lsp) enzyme which ...

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Section: Introductionmentioning

confidence: 99%

Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes

2002

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“…Embora os primeiros estudos tenham demonstrado sua localização na superfície da bactéria, dados recentes sugerem sua localização na subsuperfície (HAAKE et al, 2000;HAAKE, 2013).…”

Section: Mecanismos De Patogenicidadeunclassified

“…Tem sido observado que lipoproteínas de membrana externa e proteínas transmembranas são encontradas na fase DET, enquanto que proteínas periplasmáticas são fracionadas na fase AQ. Todo o material insolúvel ao detergente, denominado defração do cilindro protoplasmático (CP), é composto por proteínas de membrana interna e componentes citoplasmáticos (HAAKE et al, 1993;HAAKE et al, 2000;HAAKE et al, 1998;SHANG;SUMMERS;HAAKE, 1996). Desde então, essa metodologia tem sido bastante utilizada para o estudo de proteínas de membrana de leptospiras (CULLEN et al, 2003;EVANGELISTA et al, 2014;GOMEZ et al, 2008;MATSUNAGA et al, 2006;HAAKE, 2009 …”

Section: Análise Da Localização Celular Da Lic13479 Lic10050 E Lic10unclassified

Avaliação e caracterização de candidatos vacinais voltados para o controle da leptospirose.

Teixeira¹

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“…In addition to SecA, the completed genome sequence revealed the presence of all the genes of the GSP except SecB (Fraser et al, 1997). Although limited data exist on secretion mechanisms in spirochetes, the presence of GSP homologs indicates that secretion resembles that of type-II secretion found in E. coli and other Gram-negative bacteria (Haake, 2000).…”

Section: Secretory Genes In B Burgdorferimentioning

confidence: 99%

“…In other bacteria, SecA plays an integral role in passage of proteins to the outer membrane. It is believed that B. burgdorferi uses SecAdependent secretion for its multitude of outer membrane lipoproteins (Haake, 2000). The spirochete may vary its antigenic composition of surface lipoproteins by sensing and adapting to tick and mammalian environments.…”

Section: Identified E Colimentioning

confidence: 99%

Characterization of secA-sod operon in Borrellia burgdorferi.

Nichols¹

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Borrelia burgdorferi, the causative agent of Lyme disease, has been characterized as a microaerophilic spirochete. O2 consumption and utilization potentially yield reactive oxygen intermediates, such as superoxide, hydroxyl radicals, and hydrogen peroxide. This study investigated the expression of the sod gene, which encodes the only, identified oxidative defense mechanism in B. burgdorferi. Using primer extension analysis and RT-PCR, it was found that sod and secA are organized as a single transcriptional unit under the control of σ 70 -like promoter upstream of the secA open reading frame. Generally, gene expression decreases with increased distance from the promoter; however, secA expression was observed to be relatively lower amounts than sod. Both genes were expressed in all phases of growth, with greatest expression observed in stationary phase. Because transcription of most sod genes is tightly regulated by iron concentration, the secA-sod gene expression was analyzed in borrelial cells grown in varying amounts of metal. Ironrestriction did not significantly affect growth nor did it affect transcription of secA or sod.Likewise, no major differences in transcription were observed with restricting or supplementing media with manganese. To test the possibility that the borrelial SOD may function with either iron or manganese as a cofactor as in cambialistic SODs, SOD activity was assayed and the highest activity was observed in increased manganese concentrations.Protein expression profiles of Sh-2-82 cultured in metal-defined media were investigated by one-and two-dimensional gel electrophoresis. Approximately 15 proteins were differentially expressed in response to metal concentration. iv ACKNOWLEDGMENTS

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Spirochaetal lipoproteins and pathogenesis

Cited by 199 publications

References 108 publications

Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes

Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes

Avaliação e caracterização de candidatos vacinais voltados para o controle da leptospirose.

Characterization of secA-sod operon in Borrellia burgdorferi.

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