Comparative membrane proteome analysis of three <i><scp>B</scp>orrelia</i> species

Gesslbauer, Bernd; Poljak, Albina; Handwerker, Claudia; Schuler, Wolfgang; Schwendenwein, Daniel; Weber, Corinna; Lundberg, Urban; Meinke, Andreas; Kungl, Andreas J.

doi:10.1002/pmic.201100211

Cited by 28 publications

(36 citation statements)

References 66 publications

(72 reference statements)

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“…In Simkania , all but two of the 50 most abundant proteins were predicted to be associated with the outer membrane, and 63% of all detected proteins represented predicted OMPs or lipoproteins. This is a performance comparable to or better than achieved in other outer membrane proteome studies (Chung et al ., ; Thein et al ., ; Cao et al ., ; Gesslbauer et al ., ). The same enrichment protocol was much less efficient for Parachlamydia and Waddlia and consistent with a recent study on immunogenic proteins of Waddlia (Lienard et al ., ).…”

Section: Discussionmentioning

confidence: 97%

Conserved features and major differences in the outer membrane protein composition of chlamydiae

Aistleitner

Anrather

Schott

et al. 2014

Environmental Microbiology

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SummaryChlamydiae are a highly successful group of obligate intracellular bacteria infecting a variety of eukaryotic hosts. Outer membrane proteins involved in attachment to and uptake into host cells, and cross-linking of these proteins via disulfide bonds are key features of the biphasic chlamydial developmental cycle. In this study, we used a consensus approach to predict outer membrane proteins in the genomes of members of three chlamydial families. By analysing outer membrane protein fractions of purified chlamydiae with highly sensitive mass spectrometry, we show that the protein composition differs strongly between these organisms. Large numbers of major outer membrane protein-like proteins are present at high abundance in the outer membrane of Simkania negevensis and Waddlia chondrophila, whereas yet uncharacterized putative porins dominate in Parachlamydia acanthamoebae. Simkania represents the first case of a chlamydia completely lacking stabilizing cysteinerich proteins in its outer membrane. In agreement with this, and in contrast to Parachlamydia and Waddlia, the cellular integrity of Simkania is not impaired by conditions that reduce disulfide bonds of these proteins. The observed differences in the protein composition of the outer membrane among members of divergent chlamydial families suggest different stabilities of these organisms in the environment, probably due to adaption to different niches or transmission routes.

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Section: Discussionmentioning

confidence: 97%

Conserved features and major differences in the outer membrane protein composition of chlamydiae

Aistleitner

Anrather

Schott

et al. 2014

Environmental Microbiology

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“…The cells were biotinylated by sulfosuccinimidyl-6-(biotinamido) hexanoate (Sulfo-NHS-LC-Biotin; Thermo Scientific, Waltham, MA) (14,33). One liter of cultured cells was centrifuged at 12,000 ϫ g for 10 min at 4°C and then washed three times with ice-chilled PBS-1 medium consisting of 75 mM sodium phosphate (pH 7.3) and 68 mM NaCl, suspended in a 10-ml solution of Sulfo-NHS-LC-Biotin in PBS-1, and kept for 30 min on ice.…”

Section: Methodsmentioning

confidence: 99%

Whole Surface Image of Mycoplasma mobile, Suggested by Protein Identification and Immunofluorescence Microscopy

Miyata

2012

J Bacteriol

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Mycoplasma mobile, a freshwater fish pathogen featured with robust gliding motility, binds to the surface of the gill, where it then colonizes. Here, to obtain a whole image of its cell surface, we identified the proteins exposed on the surface using the following methods. (i) The cell surface was labeled with sulfosuccinimidyl-6-(biotinamido) hexanoate and recovered by an avidin column. (ii) The cells were subjected to phase partitioning using Triton X-114, and the hydrophobic proteins were recovered. (iii) The membrane fraction was analyzed by two-dimensional gel electrophoresis. These recovered proteins were subjected to peptide mass fingerprinting, and a final list of 36 expressed surface proteins was established. The ratio of identified proteins to whole surface proteins was estimated through two-dimensional gel electrophoresis of the membrane fraction. The localization of three newly found proteins, Mvsps C, E, and F, has been clarified by immunofluorescence microscopy. Integrating all information, a whole image of the cell surface showed that the proteins for gliding that were localized at the base of the protrusion of flask-shaped M. mobile account for more than 12% of all surface proteins and that Mvsps, surface variants that were localized at both parts other than the neck, account for 49% of all surface proteins.

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“…Biotinylation of surface-exposed proteins using a nonpermeable reagent combined with subsequent purification and sequencing is a well-established method to characterize the cell surface proteome of various cell types and organisms (24–26). So far, the surface proteome of only one protozoan, Trichomonas vaginalis, was analyzed by de Miguel and colleagues using the cell surface biotinylation approach.…”

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confidence: 99%

The Cell Surface Proteome of Entamoeba histolytica

Biller

Matthiesen

Kühne

et al. 2014

Molecular & Cellular Proteomics

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Surface molecules are of major importance for host-parasite interactions. During Entamoeba histolytica infections, these interactions are predicted to be of prime importance for tissue invasion, induction of colitis and liver abscess formation. To date, however, little is known about the molecules involved in these processes, with only about 20 proteins or protein families found exposed on the E. histolytica surface. We have therefore analyzed the complete surface proteome of E. histolytica. Using cell surface biotinylation and mass spectrometry, 693 putative surface-associated proteins were identified. In silico analysis predicted that ϳ26% of these proteins are membrane-associated, as they contain transmembrane domains and/or signal sequences, as well as sites of palmitoylation, myristoylation, or prenylation. An additional 25% of the identified proteins likely represent nonclassical secreted proteins. Surprisingly, no membraneassociation sites could be predicted for the remaining 49% of the identified proteins. To verify surface localization, 23 proteins were randomly selected and analyzed by immunofluorescence microscopy. Of these 23 proteins, 20 (87%) showed definite surface localization. These findings indicate that a far greater number of E. histolytica proteins than previously supposed are surface-associated, a phenomenon that may be based on the high membrane turnover of E. histolytica. Molecular & Cellular Proteomics 13: 10.1074/mcp.M113.031393, 132-144, 2014.The intestinal protozoan Entamoeba histolytica is an important human parasite. Its life cycle is relatively simple, consisting of infectious cysts that can survive outside the host and vegetative trophozoites that proliferate in the human gut. After infection, E. histolytica trophozoites are normally present in the intestine where they asymptomatically persist for months in the lumen. E. histolytica can become a pathogen by penetrating the intestinal mucosa and inducing colitis, or by disseminating to other organs, most commonly to the liver, where it induces abscess formation.The factors that determine the clinical outcomes of E. histolytica infections have not been well defined. Decisive factors may include genetic aspects of the host and/or parasite, the type of immune response mounted by the host, the presence of concomitant infections, and host diet. E. histolytica surface proteins are regarded to be of prime importance for hostparasite interactions. Members of the galactose/N-acetyl D-galactosamine-inhibitable (Gal/GalNAc) lectin family exposed on the surface of the parasite are considered important for adherence to target cells (1, 2), with adherence necessary for killing and/or phagocytosis. In addition to their involvement in adhesion and phagocytosis, the surface molecules of E. histolytica are exposed to the host's immune system. To date, only about 20 proteins or protein families have been identified as exposed on the plasma membrane of the parasite. These proteins include EhADH112 and the cysteine peptidase EhCP112 (EhCP-B9), which fo...

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Comparative membrane proteome analysis of three Borrelia species

Cited by 28 publications

References 66 publications

Conserved features and major differences in the outer membrane protein composition of chlamydiae

Conserved features and major differences in the outer membrane protein composition of chlamydiae

Whole Surface Image of Mycoplasma mobile, Suggested by Protein Identification and Immunofluorescence Microscopy

The Cell Surface Proteome of Entamoeba histolytica

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