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  • American Society for Microbiology  (147)
  • Medicine  (147)
  • 1
    Online Resource
    Online Resource
    Antibodies to Protein but Not Glycolipid Structures Are Important for Host Defense against Mycoplasma pneumoniae
    American Society for Microbiology ; 2019
    In:  Infection and Immunity Vol. 87, No. 2 ( 2019-02)
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 87, No. 2 ( 2019-02)
    Abstract: Antibody responses to Mycoplasma pneumoniae correlate with pulmonary M. pneumoniae clearance. However, M. pneumoniae -specific IgG antibodies can cross-react with the myelin glycolipid galactocerebroside (GalC) and cause neurological disorders. We assessed whether antiglycolipid antibody formation is part of the physiological immune response to M. pneumoniae . We show that antibodies against M. pneumoniae proteins and glycolipids arise in serum of M. pneumoniae -infected children and mice. Although antibodies to M. pneumoniae glycolipids were mainly IgG, anti-GalC antibodies were only IgM. B-1a cells, shown to aid in protection against pathogen-derived glycolipids, are lacking in Bruton tyrosine kinase (Btk)-deficient mice. M. pneumoniae -infected Btk-deficient mice developed M. pneumoniae -specific IgG responses to M. pneumoniae proteins but not to M. pneumoniae glycolipids, including GalC. The equal recovery from M. pneumoniae infection in Btk-deficient and wild-type mice suggests that pulmonary M. pneumoniae clearance is predominantly mediated by IgG reactive with M. pneumoniae proteins and that M. pneumoniae glycolipid-specific IgG or IgM is not essential. These data will guide the development of M. pneumoniae -targeting vaccines that avoid the induction of neurotoxic antibodies.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.00663-18
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2019
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  • 2
    Online Resource
    Online Resource
    Staphylococcus aureus CcpA Affects Biofilm Formation
    American Society for Microbiology ; 2008
    In:  Infection and Immunity Vol. 76, No. 5 ( 2008-05), p. 2044-2050
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 76, No. 5 ( 2008-05), p. 2044-2050
    Abstract: Biofilm formation in Staphylococcus aureus under in vitro growth conditions is generally promoted by high concentrations of sugar and/or salts. The addition of glucose to routinely used complex growth media triggered biofilm formation in S. aureus strain SA113. Deletion of ccpA , coding for the catabolite control protein A (CcpA), which regulates gene expression in response to the carbon source, abolished the capacity of SA113 to form a biofilm under static and flow conditions, while still allowing primary attachment to polystyrene surfaces. This suggested that CcpA mainly affects biofilm accumulation and intercellular aggregation. trans -Complementation of the mutant with the wild-type ccpA allele fully restored the biofilm formation. The biofilm produced by SA113 was susceptible to sodium metaperiodate, DNase I, and proteinase K treatment, indicating the presence of polysaccharide intercellular adhesin (PIA), protein factors, and extracellular DNA (eDNA). The investigation of several factors which were reported to influence biofilm formation in S. aureus ( arlRS , mgrA , rbf , sarA , atl , ica , citZ , citB , and cidABC ) showed that CcpA up-regulated the transcription of cidA , which was recently shown to contribute to eDNA production. Moreover, we showed that CcpA increased icaA expression and PIA production, presumably over the down-regulation of the tricarboxylic acid cycle genes citB and citZ .
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.00035-08
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2008
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  • 3
    Online Resource
    Online Resource
    The Enterohemorrhagic Escherichia coli Effector EspW Triggers Actin Remodeling in a Rac1-Dependent Manner
    American Society for Microbiology ; 2017
    In:  Infection and Immunity Vol. 85, No. 9 ( 2017-09)
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 85, No. 9 ( 2017-09)
    Abstract: Enterohemorrhagic Escherichia coli (EHEC) is a diarrheagenic pathogen that colonizes the gut mucosa and induces attaching-and-effacing lesions. EHEC employs a type III secretion system (T3SS) to translocate 50 effector proteins that hijack and manipulate host cell signaling pathways, which allow bacterial colonization and subversion of immune responses and disease progression. The aim of this study was to characterize the T3SS effector EspW. We found espW in the sequenced O157:H7 and non-O157 EHEC strains as well as in Shigella boydii . Furthermore, a truncated version of EspW, containing the first 206 residues, is present in EPEC strains belonging to serotype O55:H7. Screening a collection of clinical EPEC isolates revealed that espW is present in 52% of the tested strains. We report that EspW modulates actin dynamics in a Rac1-dependent manner. Ectopic expression of EspW results in formation of unique membrane protrusions. Infection of Swiss cells with an EHEC espW deletion mutant induces a cell shrinkage phenotype that could be rescued by Rac1 activation via expression of the bacterial guanine nucleotide exchange factor, EspT. Furthermore, using a yeast two-hybrid screen, we identified the motor protein Kif15 as a potential interacting partner of EspW. Kif15 and EspW colocalized in cotransfected cells, while ectopically expressed Kif15 localized to the actin pedestals following EHEC infection. The data suggest that Kif15 recruits EspW to the site of bacterial attachment, which in turn activates Rac1, resulting in modifications of the actin cytoskeleton that are essential to maintain cell shape during infection.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.00244-17
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2017
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  • 4
    Online Resource
    Online Resource
    Effect of staphylococcal iron content on the killing of Staphylococcus aureus by polymorphonuclear leukocytes
    American Society for Microbiology ; 1981
    In:  Infection and Immunity Vol. 32, No. 1 ( 1981-04), p. 407-410
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 32, No. 1 ( 1981-04), p. 407-410
    Abstract: Preincubation of Staphylococcus aureus 502A in broth with increasing concentrations of ferrous sulfate progressively increased their iron content, markedly increased their susceptibility to killing by hydrogen peroxide, and did not alter their susceptibility to killing by polymorphonuclear leukocytes.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.32.1.407-410.1981
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1981
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  • 5
    Online Resource
    Online Resource
    Localization of complement component 3 on Streptococcus pneumoniae: anti-capsular antibody causes complement deposition on the pneumococcal capsule
    American Society for Microbiology ; 1983
    In:  Infection and Immunity Vol. 39, No. 1 ( 1983-01), p. 403-409
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 39, No. 1 ( 1983-01), p. 403-409
    Abstract: We have previously shown that complement component 3 (C3) deposited onto encapsulated Streptococcus pneumoniae by anti-capsular antibody (Ab) is a more efficient opsonin in vitro and in vivo than C3 deposited by anti-cell wall Ab (Brown et al., J. Clin. Invest. 69:85-98, 1982). In the present study, we explored the cellular location of C3b molecules that differ in opsonic efficiency by using avidin-ferritin to localize biotinylated Ab and C3 molecules on S. pneumoniae for electron microscopy. Anti-cell wall Ab and C3b molecules deposited by this Ab on unencapsulated S. pneumoniae were localized to S. pneumoniae cell walls. Anti-capsular Ab and C3b deposited by this Ab were seen in clusters on encapsulated S. pneumoniae at a distance from the cell wall. However, no avidin-ferritin staining of encapsulated S. pneumoniae was seen on incubation with biotinyl-anti-cell wall Ab, biotinylated C3 fixed by anti-cell wall Ab, or nonimmune serum containing biotinyl-C3. In each case, uptake of the biotinylated component was proven by radioactivity measurements, since biotinylated Ab and C3 were also radiolabeled with 125I. When avidin-ferritin did not bind to biotinylated components. Ouchterlony analysis indicated that C3 was bound to cell wall components on the encapsulated organisms. Thus, we conclude that, for encapsulated S. pneumoniae, opsonically efficient C3b molecules, deposited by anti-capsular Ab, are located on the S. pneumoniae capsule, whereas the opsonically inefficient C3b molecules deposited by anti-cell wall Ab or nonimmune serum are located on the cell wall. A major reason for the increased virulence of encapsulated compared to unencapsulated S. pneumoniae is that, in the absence of anti-capsular Ab, the S. pneumoniae capsule interferes with the recognition of cell wall-bound C3b molecules by phagocytic cell receptors.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.39.1.403-409.1983
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1983
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    TH Wildau
    FH Potsdam
  • 6
    Online Resource
    Online Resource
    Decrease of the lymphoproliferative response to varicella-zoster virus antigen in the aged
    American Society for Microbiology ; 1981
    In:  Infection and Immunity Vol. 32, No. 1 ( 1981-04), p. 24-27
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 32, No. 1 ( 1981-04), p. 24-27
    Abstract: Humoral antibodies and specific cellular immune reactions (proliferative immune response in the lymphocyte transformation test) to varicella-zoster virus antigen were measured in children, young adults, and elderly people. In children and young adults, the humoral varicella-zoster-specific antibodies and the virus-specific cellular immune response generally coincided. In the over-60 age group, however, a discrepancy was often observed between these parameters. Ninety percent of the elderly subjects showed humoral antibodies, but only 64% still had a measurable varicella-zoster-specific immune response. There was no correlation between the magnitude of the virus antigen-specific immune response and the mitogen-induced lymphoproliferative response (phytohemagglutinin stimulation). One in three elderly people, therefore, showed no cellular immune response to the varicella-zoster virus antigen, and this person could probably be regarded as a potential herpes zoster patient.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.32.1.24-27.1981
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1981
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  • 7
    Online Resource
    Online Resource
    σ B and the σ B -Dependent arlRS and yabJ-spoVG Loci Affect Capsule Formation in Staphylococcus aureus
    American Society for Microbiology ; 2007
    In:  Infection and Immunity Vol. 75, No. 9 ( 2007-09), p. 4562-4571
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 75, No. 9 ( 2007-09), p. 4562-4571
    Abstract: The alternative transcription factor σ B of Staphylococcus aureus affects the transcription of the cap gene cluster, required for the synthesis of capsular polysaccharide (CP), although this operon is lacking an apparent σ B -dependent promoter. Regulation of cap expression and CP production in S. aureus strain Newman was shown here to be influenced by σ B , the two-component signal transduction regulatory system ArlRS, and the yabJ-spoVG locus to different extents. Inactivation of arlR or deletion of the sigB operon strongly suppressed capA (CP synthesis enzyme A) transcription. Deletion of spoVG had a polar effect on yabJ-spoVG transcription and resulted in a two- to threefold decrease in capA transcription. Interestingly, immunofluorescence showed that CP production was strongly impaired in all three mutants, signaling that the yabJ-spoVG inactivation, despite its only partial effect on capA transcription, abolished capsule formation. trans -Complementation of the Δ spoVG mutant with yabJ-spoVG under the control of its native promoter restored CP-5 production and capA expression to levels seen in the wild type. Northern analyses revealed a strong impact of σ B on arlRS and yabJ-spoVG transcription. We hypothesize that ArlR and products of the yabJ-spoVG locus may serve as effectors that modulate σ B control over σ B -dependent genes lacking an apparent σ B promoter.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.00392-07
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2007
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  • 8
    Online Resource
    Online Resource
    Serum antibodies against gangliosides and Campylobacter jejuni lipopolysaccharides in Miller Fisher syndrome
    American Society for Microbiology ; 1997
    In:  Infection and Immunity Vol. 65, No. 10 ( 1997-10), p. 4038-4042
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 65, No. 10 ( 1997-10), p. 4038-4042
    Abstract: Seven patients with Miller Fisher syndrome (MFS), six in the acute phase and one in the recovery phase, were investigated for serum antibodies against gangliosides and purified lipopolysaccharides (LPS) from different strains of Campylobacter jejuni, including the MFS-associated serotypes O:2 and O:23. Immunoglobulin G antibodies against gangliosides GT1a and GQ1b were found in five of six patients in the acute phase of disease. Three of these patients also displayed antibodies to ganglioside GD2, a finding not previously reported for MFS. All anti-GT1a- and anti-GQ1b-seropositive patients showed antibody binding to C. jejuni LPS, predominantly to O:2 and O:23 LPS. Antibody cross-reactivity between gangliosides GT1a and GQ1b and O:2 and O:23 LPS was demonstrated by adsorption studies. This cross-reactivity between gangliosides and C.jejuni LPS, which is obviously due to oligosaccharide homologies, may be an important pathogenetic factor in the development of MFS after C. jejuni infection.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.65.10.4038-4042.1997
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1997
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  • 9
    Online Resource
    Online Resource
    Endotoxin Binding and Elimination by Monocytes: Secretion of Soluble CD14 Represents an Inducible Mechanism Counteracting Reduced Expression of Membrane CD14 in Patients with Sepsis and in a Patient with Paroxysmal Nocturnal Hemoglobinuria
    American Society for Microbiology ; 1998
    In:  Infection and Immunity Vol. 66, No. 3 ( 1998-03), p. 1135-1141
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 66, No. 3 ( 1998-03), p. 1135-1141
    Abstract: Little is known about the role of peripheral blood mononuclear cells (PBMCs) in lipopolysaccharide (LPS) elimination. We studied the endotoxin elimination capacities (EEC) of PBMCs of 15 healthy volunteers, 13 patients with sepsis, and 1 patient suffering from paroxysmal nocturnal hemoglobinuria (PNH). Although expression of CD14, the best-characterized receptor for LPS to date, was reduced from 93.6% ± 0.8% in healthy subjects to 50.5% ± 6.5% in patients with sepsis and was 0.3% in a patient with septic PNH, EEC were found to be unchanged. There was no difference in the amount of tumor necrosis factor alpha (TNF-α) released by PBMCs of healthy donors and patients with sepsis. Anti-CD14 antibodies (MEM-18) completely suppressed EEC, binding of fluorescein isothiocyanate-labeled LPS to monocytes as determined by FACScan analysis, and TNF-α release in all three groups studied. The concentrations of soluble CD14 (sCD14) secreted by endotoxin-stimulated PBMCs from healthy donors and patients with sepsis amounted to 4.5 ± 0.4 and 20.1 ± 1.8 ng/ml, respectively. Based on our results, we suggest that PBMCs eliminate LPS by at least two different mechanisms; in healthy subjects, the membrane CD14 (mCD14) receptor is the most important factor for LPS elimination, while in patients with sepsis (including the septic state of PNH), increased sCD14 participates in LPS elimination. Secretion of sCD14 is strongly enhanced under conditions of low expression of mCD14 in order to counteract the reduction of mCD14 and maintain the function of monocytes. This sCD14 may substitute the role of mCD14 in LPS elimination during sepsis. The elimination of LPS by PBMCs correlates with the binding reaction and the secretion of TNF-α.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.66.3.1135-1141.1998
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1998
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  • 10
    Online Resource
    Online Resource
    Zipper-Like Internalization of Dr-Positive Escherichia coli by Epithelial Cells Is Preceded by an Adhesin-Induced Mobilization of Raft-Associated Molecules in the Initial Step of Adhesion
    American Society for Microbiology ; 2004
    In:  Infection and Immunity Vol. 72, No. 7 ( 2004-07), p. 3733-3742
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 72, No. 7 ( 2004-07), p. 3733-3742
    Abstract: We undertook a study of the mechanism by which Dr-positive bacteria invade epithelial cells. Our findings show that Dr-positive bacteria enter via a zipper-like mechanism that is independent of the Dr-induced mobilization of F-actin and of the signaling molecules that control Dr-induced F-actin rearrangements. We also observed that Dr-positive IH11128 bacteria entered cells that were positive for the caveola marker VIP21/caveolin (HeLa and Caco-2/Cav-1 cells) to the same extent as those that were not (parental Caco-2 cells). Using fluorescence labeling and confocal laser scanning microscopy, we provide evidence that during the adhesion step, the α5β1 integrin, which plays a pivotal role in Afa/Dr diffusely adhering Escherichia coli bacterial entry, is mobilized around adhering Dr-positive bacteria. We show that the receptor for Afa/Dr adhesins, glycosylphosphatidylinositol-anchored CD55; the raft marker, ganglioside GM1; and VIP21/caveolin are all recruited around adhering Dr-positive bacteria. We also observed that extracting membrane cholesterol with methyl-β-cyclodextrin (MBCD) did not affect the recruitment of CD55, GM1, or β1 integrin to adhering Dr-positive bacteria. In contrast, extracting or changing membrane-bound cholesterol by means of drugs that modify lipid rafts (MBCD, filipin III, or mevalonate plus lovastatin plus MBCD) inhibited the entry of Dr-positive IH11128 both into cells that expressed VIP21/caveolin (HeLa and Caco-2/Cav-1 cells) and into those that did not (parental Caco-2 cells). Finally, restoring cholesterol within the cell membrane of MBCD-treated cells restored Dr-positive IH11128 internalization.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.72.7.3733-3742.2004
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2004
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