Biogenesis of Membrane Lipoproteins in Bacteria

1984 ◽  
pp. 19-31
Author(s):  
Henry C. Wu
Keyword(s):  
Membrane Lipoproteins

scholarly journals Characterization of new membrane lipoproteins and their precursors of Escherichia coli.

1981 ◽  
Vol 256 (6) ◽  
pp. 3125-3129
Author(s):  
S. Ichihara ◽  
M. Hussain ◽  
S. Mizushima
Keyword(s):  
Escherichia Coli ◽  
Membrane Lipoproteins

scholarly journals Cofactor bypass variants reveal a conformational control mechanism governing cell wall polymerase activity

2016 ◽  
Vol 113 (17) ◽  
pp. 4788-4793 ◽  
Author(s):  
Monica Markovski ◽  
Jessica L. Bohrhunter ◽  
Tania J. Lupoli ◽  
Tsuyoshi Uehara ◽  
Suzanne Walker ◽  
...  
Keyword(s):  
Polymerase Activity ◽  
Activation Mechanism ◽  
Phenotypic Analysis ◽  
Outer Membranes ◽  
Division Site ◽  
Physiological Relevance ◽  
Membrane Lipoproteins ◽  
Shed Light

To fortify their cytoplasmic membrane and protect it from osmotic rupture, most bacteria surround themselves with a peptidoglycan (PG) exoskeleton synthesized by the penicillin-binding proteins (PBPs). As their name implies, these proteins are the targets of penicillin and related antibiotics. We and others have shown that the PG synthases PBP1b and PBP1a ofEscherichia colirequire the outer membrane lipoproteins LpoA and LpoB, respectively, for their in vivo function. Although it has been demonstrated that LpoB activates the PG polymerization activity of PBP1b in vitro, the mechanism of activation and its physiological relevance have remained unclear. We therefore selected for variants of PBP1b (PBP1b*) that bypass the LpoB requirement for in vivo function, reasoning that they would shed light on LpoB function and its activation mechanism. Several of these PBP1b variants were isolated and displayed elevated polymerization activity in vitro, indicating that the activation of glycan polymer growth is indeed one of the relevant functions of LpoB in vivo. Moreover, the location of amino acid substitutions causing the bypass phenotype on the PBP1b structure support a model in which polymerization activation proceeds via the induction of a conformational change in PBP1b initiated by LpoB binding to its UB2H domain, followed by its transmission to the glycosyl transferase active site. Finally, phenotypic analysis of strains carrying a PBP1b* variant revealed that the PBP1b–LpoB complex is most likely not providing an important physical link between the inner and outer membranes at the division site, as has been previously proposed.

Protein typing of major outer membrane lipoproteins from Chinese pathogenic Leptospira spp. and characterization of their immunogenicity

Vaccine ◽  
2009 ◽  
Vol 28 (1) ◽  
pp. 243-255 ◽  
Author(s):  
Dongjiao Luo ◽  
Feng Xue ◽  
David M. Ojcius ◽  
Jinfang Zhao ◽  
Yafei Mao ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Pathogenic Leptospira ◽  
Leptospira Spp ◽  
Membrane Lipoproteins

Cytoplasmic Membrane Lipoprotein LppC ofStreptococcus equisimilis Functions as an Acid Phosphatase

1998 ◽  
Vol 64 (7) ◽  
pp. 2439-2442 ◽  
Author(s):  
Horst Malke
Keyword(s):  
Acid Phosphatase ◽  
Cell Membrane ◽  
Cytoplasmic Membrane ◽  
Structural Homology ◽  
Whole Cells ◽  
Specific Enzymatic Activity ◽  
Acidic Conditions ◽  
Membrane Lipoprotein ◽  
Triton X ◽  
Membrane Lipoproteins

ABSTRACT The function of the streptococcal cytoplasmic membrane lipoprotein, LppC, was identified with isogenic Streptococcus equisimilis H46A and Escherichia coli JM109 strain pairs differing in whether they contained [H46A and JM109(pLPP2)] or lacked (H46A lppC::pLPP10 and JM109) the functional lppC gene for comparative phosphatase determinations under acidic conditions. lppC-directed acid phosphatase activity was demonstrated zymographically and by specific enzymatic activity assays, with whole cells or cell membrane preparations as enzyme sources. LppC acid phosphatase showed optimum activity at pH 5, and the enzyme activity was unaffected by Triton X-100, l-(+)-tartaric acid, or EDTA. Database searches revealed significant structural homology of LppC to the Streptococcus pyogenes LppA,Flavobacterium meningosepticum OplA, Helicobacter pylori HP1285, and Haemophilus influenzae Hel [e (P4)] proteins. These results suggest a possible function for these proteins and establish a novel function of streptococcal cell membrane lipoproteins.

scholarly journals Two Outer Membrane Lipoproteins from Histophilus somni Are Immunogenic in Rabbits and Sheep and Induce Protection against Bacterial Challenge in Mice

2012 ◽  
Vol 19 (11) ◽  
pp. 1826-1832 ◽  
Author(s):  
Carolina Guzmán-Brambila ◽  
Argelia E. Rojas-Mayorquín ◽  
Beatriz Flores-Samaniego ◽  
Daniel Ortuño-Sahagún
Keyword(s):  
Well Being ◽  
Economic Loss ◽  
Bacterial Challenge ◽  
Content Type ◽  
Feeder Cattle ◽  
Histophilus Somni ◽  
Antibody Titers ◽  
First Time ◽  
Membrane Lipoproteins ◽  
Health And Well Being

ABSTRACTHistophilus somniis an economically important pathogen of cattle and other ruminants and is considered one of the key components of the bovine respiratory disease (BRD) complex, the leading cause of economic loss in the livestock industry. BRD is a multifactorial syndrome, in which a triad of agents, including bacteria, viruses, and predisposing factors or “stressors,” combines to induce disease. Although vaccines againstH. somnihave been used for many decades, traditional bacterins have failed to demonstrate effective protection in vaccinated animals. Hence, the BRD complex continues to produce strong adverse effects on the health and well-being of stock and feeder cattle. The generation of recombinant proteins may facilitate the development of more effective vaccines againstH. somni, which could confer better protection against BRD. In the present study, primers were designed to amplify, clone, express, and purify two recombinant lipoproteins fromH. somni, p31 (Plp4) and p40 (LppB), which are structural proteins of the outer bacterial membrane. The results presented here demonstrate, to our knowledge for the first time, that when formulated, an experimental vaccine enriched with these two recombinant lipoproteins generates high antibody titers in rabbits and sheep and exerts a protective effect in mice against septicemia induced byH. somnibacterial challenge.

scholarly journals Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface

2017 ◽  
Vol 199 (6) ◽  
Author(s):  
Alexander S. Dowdell ◽  
Maxwell D. Murphy ◽  
Christina Azodi ◽  
Selene K. Swanson ◽  
Laurence Florens ◽  
...  
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Outer Membrane ◽  
Protein Localization ◽  
Human Pathogen ◽  
Expression Library ◽  
Content Type ◽  
Bacterial Surface ◽  
Host Pathogen ◽  
Membrane Lipoproteins

ABSTRACT The Lyme disease spirochete Borrelia burgdorferi is unique among bacteria in its large number of lipoproteins that are encoded by a small, exceptionally fragmented, and predominantly linear genome. Peripherally anchored in either the inner or outer membrane and facing either the periplasm or the external environment, these lipoproteins assume varied roles. A prominent subset of lipoproteins functioning as the apparent linchpins of the enzootic tick-vertebrate infection cycle have been explored as vaccine targets. Yet, most of the B. burgdorferi lipoproteome has remained uncharacterized. Here, we comprehensively and conclusively localize the B. burgdorferi lipoproteome by applying established protein localization assays to a newly generated epitope-tagged lipoprotein expression library and by validating the obtained individual protein localization results using a sensitive global mass spectrometry approach. The derived consensus localization data indicate that 86 of the 125 analyzed lipoproteins encoded by B. burgdorferi are secreted to the bacterial surface. Thirty-one of the remaining 39 periplasmic lipoproteins are retained in the inner membrane, with only 8 lipoproteins being anchored in the periplasmic leaflet of the outer membrane. The localization of 10 lipoproteins was further defined or revised, and 52 surface and 23 periplasmic lipoproteins were newly localized. Cross-referencing prior studies revealed that the borrelial surface lipoproteome contributing to the host-pathogen interface is encoded predominantly by plasmids. Conversely, periplasmic lipoproteins are encoded mainly by chromosomal loci. These studies close a gap in our understanding of the functional lipoproteome of an important human pathogen and set the stage for more in-depth studies of thus-far-neglected spirochetal lipoproteins. IMPORTANCE The small and exceptionally fragmented genome of the Lyme disease spirochete Borrelia burgdorferi encodes over 120 lipoproteins. Studies in the field have predominantly focused on a relatively small number of surface lipoproteins that play important roles in the transmission and pathogenesis of this global human pathogen. Yet, a comprehensive spatial assessment of the entire borrelial lipoproteome has been missing. The current study newly identifies 52 surface and 23 periplasmic lipoproteins. Overall, two-thirds of the B. burgdorferi lipoproteins localize to the surface, while outer membrane lipoproteins facing the periplasm are rare. This analysis underscores the dominant contribution of lipoproteins to the spirochete's rather complex and adaptable host-pathogen interface, and it encourages further functional exploration of its lipoproteome.

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