Comparative Proteomic Analysis of the
            <i>Haemophilus ducreyi</i>
            Porin-Deficient Mutant 35000HP::P2AB

Davie, J.; Campagnari, Anthony A.

doi:10.1128/jb.01487-08

Cited by 4 publications

(4 citation statements)

References 56 publications

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“…76, 121, and 124), and DNA binding proteins (no. 96, 115) were detected in outer membrane [ 52 , 64 – 66 ] and OMV fractions [ 52 , 67 ]. The possible mechanisms for their OMV inclusion may involve association of the cytoplasmic proteins with membrane proteins that may bring the former to membrane proximity.…”

Section: Discussionmentioning

confidence: 99%

Vesiculation fromPseudomonas aeruginosaunder SOS

Maredia

Devineni

Lentz

et al. 2012

The Scientific World Journal

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Bacterial infections can be aggravated by antibiotic treatment that induces SOS response and vesiculation. This leads to a hypothesis concerning association of SOS with vesiculation. To test it, we conducted multiple analyses of outer membrane vesicles (OMVs) produced from thePseudomonas aeruginosawild type in which SOS is induced by ciprofloxacin and from the LexA noncleavable (lexAN) strain in which SOS is repressed. The levels of OMV proteins, lipids, and cytotoxicity increased for both the treated strains, demonstrating vesiculation stimulation by the antibiotic treatment. However, the further increase was suppressed in thelexANstrains, suggesting the SOS involvement. Obviously, the stimulated vesiculation is attributed by both SOS-related and unrelated factors. OMV subproteomic analysis was performed to examine these factors, which reflected the OMV-mediated cytotoxicity and the physiology of the vesiculating cells under treatment and SOS. Thus, SOS plays a role in the vesiculation stimulation that contributes to cytotoxicity.

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Section: Discussionmentioning

confidence: 99%

Vesiculation fromPseudomonas aeruginosaunder SOS

Maredia

Devineni

Lentz

et al. 2012

The Scientific World Journal

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“…For example, in Haemophilus species, omp A, which maintains cell structure and functions as a porin regulating the entry of nutrients into the bacterium, has been well established [ 37 ]. Additionally, OMP- or porin-deficient mutant strains have shown reduced growth or loss of viability in Mycobacterium species [ 24 ], Salmonella enterica [ 5 ], Haemophilus ducreyi [ 10 ], and E. coli [ 9 ].…”

Section: Discussionmentioning

confidence: 99%

Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficientBartonella henselae

Kang

Lee

et al. 2018

J Vet Sci

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Outer membrane proteins (OMPs) of Gram-negative bacteria constitute the first line of defense protecting cells against environmental stresses including chemical, biophysical, and biological attacks. Although the 43-kDa OMP (OMP43) is major porin protein among Bartonella henselae-derived OMPs, its function remains unreported. In this study, OMP43-deficient mutant B. henselae (Δomp43) was generated to investigate OMP43 function. Interestingly, Δomp43 exhibited weaker proliferative ability than that of wild-type (WT) B. henselae. To study the differences in proteomic expression between WT and Δomp43, two-dimensional gel electrophoresis-based proteomic analysis was performed. Based on Clusters of Orthologus Groups functional assignments, 12 proteins were associated with metabolism, 7 proteins associated with information storage and processing, and 3 proteins associated with cellular processing and signaling. By semi-quantitative reverse transcriptase polymerase chain reaction, increases in tldD, efp, ntrX, pdhA, purB, and ATPA mRNA expression and decreases in Rho and yfeA mRNA expression were confirmed in Δomp43. In conclusion, this is the first report showing that a loss of OMP43 expression in B. henselae leads to retarded proliferation. Furthermore, our proteomic data provide useful information for the further investigation of mechanisms related to the growth of B. henselae.

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“…Whether the C-terminal YRF sequence of OpnS is involved in sensing membrane perturbations in X. nematophila remains to be determined. In Haemophilus ducreyi deletion of the porins OmpP2A and OmpP2B enhanced sensitivity to erythromycin, antimicrobial compounds, and several detergents (8). Proteomic comparison between membrane proteins of the parent and the ompP2AB porin-deficient strain revealed that the absence of porins stimulated a global response in which numerous proteins of diverse function were differentially expressed in the mutant strain.…”

Section: Discussionmentioning

confidence: 99%

OpnS, an Outer Membrane Porin ofXenorhabdus nematophila, Confers a Competitive Advantage for Growth in the Insect Host

Hoeven

Forst

2009

J Bacteriol

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The gammaproteobacterium Xenorhabdus nematophila engages in a mutualistic association with an entomopathogenic nematode and also functions as a pathogen toward different insect hosts. We studied the role of the growth-phase-regulated outer membrane protein OpnS in host interactions. OpnS was shown to be a 16-stranded ␤-barrel porin. opnS was expressed during growth in insect hemolymph and expression was elevated as the cell density increased. When wild-type and opnS deletion strains were coinjected into insects, the wild-type strain was predominantly recovered from the insect cadaver. Similarly, an opnS-complemented strain outcompeted the ⌬opnS strain. Coinjection of the wild-type and ⌬opnS strains together with uncolonized nematodes into insects resulted in nematode progeny that were almost exclusively colonized with the wild-type strain. Likewise, nematode progeny recovered after coinjection of a mixture of nematodes carrying either the wild-type or ⌬opnS strain were colonized by the wild-type strain. In addition, the ⌬opnS strain displayed a competitive growth defect when grown together with the wild-type strain in insect hemolymph but not in defined culture medium. The ⌬opnS strain displayed increased sensitivity to antimicrobial compounds, suggesting that deletion of OpnS affected the integrity of the outer membrane. These findings show that the OpnS porin confers a competitive advantage for the growth and/or the survival of X. nematophila in the insect host and provides a new model for studying the biological relevance of differential regulation of porins in a natural host environment.

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Comparative Proteomic Analysis of the Haemophilus ducreyi Porin-Deficient Mutant 35000HP::P2AB

Cited by 4 publications

References 56 publications

Vesiculation fromPseudomonas aeruginosaunder SOS

Vesiculation fromPseudomonas aeruginosaunder SOS

Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficientBartonella henselae

OpnS, an Outer Membrane Porin ofXenorhabdus nematophila, Confers a Competitive Advantage for Growth in the Insect Host

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