<i><scp>O</scp></i>‐linked protein glycosylation in mycoplasma

Jordan, David S.; Daubenspeck, James M.; Laube, Audra H.; Renfrow, Matthew B.; Dybvig, Kevin

doi:10.1111/mmi.12415

Cited by 9 publications

(16 citation statements)

References 37 publications

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“…The unique expansion of the polyserine repeat may cause this phenotype by changing the way P1 folds or by changing its flexibility, and therefore its interactions with other proteins in the adhesin complex. As protein glycosylation at serine residues has recently been described in mycoplasma, the serine repeat might be a region that is heavily glycosylated with potential consequences on P1 function [ 63 ].…”

Section: Discussionmentioning

confidence: 99%

Comparative genome analysis of Mycoplasma pneumoniae

et al. 2015

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BackgroundMycoplasma pneumoniae is a common pathogen that causes upper and lower respiratory tract infections in people of all ages, responsible for up to 40 % of community-acquired pneumonias. It also causes a wide array of extrapulmonary infections and autoimmune phenomena. Phylogenetic studies of the organism have been generally restricted to specific genes or regions of the genome, because whole genome sequencing has been completed for only 4 strains. To better understand the physiology and pathogenicity of this important human pathogen, we performed comparative genomic analysis of 15 strains of M. pneumoniae that were isolated between the 1940s to 2009 from respiratory specimens and cerebrospinal fluid originating from the USA, China and England.ResultsIllumina MiSeq whole genome sequencing was performed on the 15 strains and all genome sequences were completed. Results from the comparative genomic analysis indicate that although about 1500 SNP and indel variants exist between type1 and type 2 strains, there is an overall high degree of sequence similarity among the strains (>99 % identical to each other). Within the two subtypes, conservation of most genes, including the CARDS toxin gene and arginine deiminase genes, was observed. The major variation occurs in the P1 and ORF6 genes associated with the adhesin complex. Multiple hsdS genes (encodes S subunit of type I restriction enzyme) with variable tandem repeat copy numbers were found in all 15 genomes.ConclusionsThese data indicate that despite conclusions drawn from 16S rRNA sequences suggesting rapid evolution, the M. pneumoniae genome is extraordinarily stable over time and geographic distance across the globe with a striking lack of evidence of horizontal gene transfer.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-015-1801-0) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Comparative genome analysis of Mycoplasma pneumoniae

et al. 2015

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“…Among this family of proteins is the Fap1 protein of Streptococcus parasanguinis and the human platelet binding protein GspB of Streptococcus gordonii , which both undergo O-linked glycosylation [ 63 ]. Glycosylation of mycoplasma proteins has been documented, although the function of these modifications has not been defined; for example, an abundance of O-linked glycosylated serine and threonine residues was recently identified in proteins of Mycoplasma arthritidis [ 64 ]. In other bacterial species glycosylated bacterial proteins serve multiple purposes including enhanced attachment in Chlamydia trachomatis [ 65 ], immunomodulation through glycomimicry in group A and group B streptococci, Neisseria meningitidis , and E .…”

Section: Discussionmentioning

confidence: 99%

Analysis of the Mycoplasma genitalium MgpB Adhesin to Predict Membrane Topology, Investigate Antibody Accessibility, Characterize Amino Acid Diversity, and Identify Functional and Immunogenic Epitopes

2015

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Mycoplasma genitalium is a sexually transmitted pathogen and is associated with reproductive tract disease that can be chronic in nature despite the induction of a strong antibody response. Persistent infection exacerbates the likelihood of transmission, increases the risk of ascension to the upper tract, and suggests that M. genitalium may possess immune evasion mechanism(s). Antibodies from infected patients predominantly target the MgpB adhesin, which is encoded by a gene that recombines with homologous donor sequences, thereby generating sequence variation within and among strains. We have previously characterized mgpB heterogeneity over the course of persistent infection and have correlated the induction of variant-specific antibodies with the loss of that particular variant from the infected host. In the current study, we examined the membrane topology, antibody accessibility, distribution of amino acid diversity, and the location of functional and antigenic epitopes within the MgpB adhesin. Our results indicate that MgpB contains a single transmembrane domain, that the majority of the protein is surface exposed and antibody accessible, and that the attachment domain is located within the extracellular C-terminus. Not unexpectedly, amino acid diversity was concentrated within and around the three previously defined variable regions (B, EF, and G) of MgpB; while nonsynonymous mutations were twice as frequent as synonymous mutations in regions B and G, region EF had equal numbers of nonsynonymous and synonymous mutations. Interestingly, antibodies produced during persistent infection reacted predominantly with the conserved C-terminus and variable region B. In contrast, infection-induced antibodies reacted poorly with the N-terminus, variable regions EF and G, and intervening conserved regions despite the presence of predicted B cell epitopes. Overall, this study provides an important foundation to define how different segments of the MgpB adhesin contribute to functionality, variability, and immunogenicity during persistent M. genitalium infection.

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“…M . arthritidis strain TnCtrl, derived from strain 158, was used here and for previous studies on protein glycosylation [ 11 , 15 , 16 ]. It was cultured in serum-free medium [ 12 ].…”

Section: Methodsmentioning

confidence: 99%

“…Protein bands were excised and subjected to in-gel tryptic digestion. The samples were subjected to LC-HR-MS using the instrumentation and methods as described [ 11 ]. The mass spectra were analyzed by using the PEAKS 7 proteomics software (Bioinformatics Solutions, Inc.).…”

Section: Methodsmentioning

confidence: 99%

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General N-and O-Linked Glycosylation of Lipoproteins in Mycoplasmas and Role of Exogenous Oligosaccharide

Daubenspeck¹,

Jordan²,

Simmons³

et al. 2015

PLoS ONE

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The lack of a cell wall, flagella, fimbria, and other extracellular appendages and the possession of only a single membrane render the mycoplasmas structurally simplistic and ideal model organisms for the study of glycoconjugates. Most species have genomes of about 800 kb and code for few proteins predicted to have a role in glycobiology. The murine pathogens Mycoplasma arthritidis and Mycoplasma pulmonis have only a single gene annotated as coding for a glycosyltransferase but synthesize glycolipid, polysaccharide and glycoproteins. Previously, it was shown that M. arthritidis glycosylated surface lipoproteins through O-linkage. In the current study, O-linked glycoproteins were similarly found in M. pulmonis and both species of mycoplasma were found to also possess N-linked glycans at residues of asparagine and glutamine. Protein glycosylation occurred at numerous sites on surface-exposed lipoproteins with no apparent amino acid sequence specificity. The lipoproteins of Mycoplasma pneumoniae also are glycosylated. Glycosylation was dependent on the glycosidic linkages from host oligosaccharides. As far as we are aware, N-linked glycoproteins have not been previously described in Gram-positive bacteria, the organisms to which the mycoplasmas are phylogenetically related. The findings indicate that the mycoplasma cell surface is heavily glycosylated with implications for the modulation of mycoplasma-host interactions.

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O‐linked protein glycosylation in mycoplasma

Cited by 9 publications

References 37 publications

Comparative genome analysis of Mycoplasma pneumoniae

Comparative genome analysis of Mycoplasma pneumoniae

Analysis of the Mycoplasma genitalium MgpB Adhesin to Predict Membrane Topology, Investigate Antibody Accessibility, Characterize Amino Acid Diversity, and Identify Functional and Immunogenic Epitopes

General N-and O-Linked Glycosylation of Lipoproteins in Mycoplasmas and Role of Exogenous Oligosaccharide

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