A Mutation Affecting Expression of a Major Outer Membrane Protein of Moraxella catarrhalis Alters Serum Resistance and Survival In Vivo

1993 ◽  
Vol 168 (5) ◽  
pp. 1194-1201 ◽  
Author(s):  
M. E. Helminen ◽  
I. Maciver ◽  
M. Paris ◽  
J. L. Latimer ◽  
S. L. Lumbley ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Moraxella Catarrhalis ◽  
Major Outer Membrane Protein ◽  
Serum Resistance

scholarly journals In Vivo Transfer of Plasmid-Encoded ACC-1 AmpC from Klebsiella pneumoniae to Escherichia coli in an Infant and Selection of Impermeability to Imipenem in K. pneumoniae

2005 ◽  
Vol 49 (8) ◽  
pp. 3562-3565 ◽  
Author(s):  
Philippe Bidet ◽  
Béatrice Burghoffer ◽  
Valérie Gautier ◽  
Naïma Brahimi ◽  
Patricia Mariani-Kurkdjian ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Klebsiella Pneumoniae ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Major Outer Membrane Protein ◽  
In Vivo Selection ◽  
Selection Of

ABSTRACT We describe in vivo selection of a Klebsiella pneumoniae strain with diminished imipenem susceptibility attributable to plasmid-encoded ACC-1 β-lactamase production and loss of a 36-kDa major outer membrane protein, together with transfer of this plasmid from K. pneumoniae to Escherichia coli in a Tunisian infant.

scholarly journals LipL32 Is an Extracellular Matrix-Interacting Protein of Leptospira spp. and Pseudoalteromonas tunicata

2008 ◽  
Vol 76 (5) ◽  
pp. 2063-2069 ◽  
Author(s):  
David E. Hoke ◽  
Suhelen Egan ◽  
Paul A. Cullen ◽  
Ben Adler
Keyword(s):  
Extracellular Matrix ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Outer Membrane Proteins ◽  
Major Outer Membrane Protein ◽  
Interacting Proteins ◽  
Orthologous Protein ◽  
Pseudoalteromonas Tunicata

ABSTRACT LipL32 is the major outer membrane protein in pathogenic Leptospira. It is highly conserved throughout pathogenic species and is expressed in vivo during human infection. While these data suggest a role in pathogenesis, a function for LipL32 has not been defined. Outer membrane proteins of gram-negative bacteria are the first line of molecular interaction with the host, and many have been shown to bind host extracellular matrix (ECM). A search for leptospiral ECM-interacting proteins identified the major outer membrane protein, LipL32. To verify this finding, recombinant LipL32 was expressed in Escherichia coli and was found to bind Matrigel ECM and individual components of ECM, including laminin, collagen I, and collagen V. Likewise, an orthologous protein found in the genome of Pseudoalteromonas tunicata strain D2 was expressed and found to be functionally similar and immunologically cross-reactive. Lastly, binding activity was mapped to the C-terminal 72 amino acids. These studies show that LipL32 and an orthologous protein in P. tunicata are immunologically cross-reactive and function as ECM-interacting proteins via a conserved C-terminal region.

scholarly journals Induction of Protective Immunity against Chlamydia trachomatis Genital Infection by a Vaccine Based on Major Outer Membrane Protein–Lipophilic Immune Response-Stimulating Complexes

2000 ◽  
Vol 68 (12) ◽  
pp. 6798-6806 ◽  
Author(s):  
Joseph U. Igietseme ◽  
Andrew Murdin
Keyword(s):  
Immune Response ◽  
Chlamydia Trachomatis ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Major Outer Membrane Protein ◽  
Genital Infection ◽  
Th1 Cell ◽  
Th1 Response

ABSTRACT The significance of delivery systems in modern vaccine design strategies is underscored by the fact that a promising vaccine formulation may fail in vivo due to an inappropriate delivery method. We evaluated the immunogenicity and efficacy of a candidate vaccine comprising the major outer membrane protein (MOMP) of Chlamydia trachomatis delivered with the lipophilic immune response-stimulating complexes (ISCOMs) as a vehicle with adjuvant properties, in a murine model of chlamydial genital infection. Immunocompetent BALB/c mice were immunized intranasally (IN) or intramuscularly (IM) with MOMP, MOMP-ISCOMs, and live or heat-inactivated C. trachomatis serovar D. The level of local genital mucosal Th1 response was measured by assaying for antigen-specific Th1 cell induction and recruitment into the genital mucosa at different times after immunization. Immunization with MOMP-ISCOMs by the IM route induced the greatest and fastest local genital mucosal Th1 response, first detectable 2 weeks after exposure. Among the other routes and regimens tested, only IN immunization with MOMP-ISCOMs induced detectable and statistically significant levels of local genital mucosal Th1 response during the 8-week test period (P < 0.001). In addition, when T cells from immunized mice were adoptively transferred into syngeneic naive animals and challenged intravaginally with Chlamydia, recipients of IM immunization of MOMP-ISCOMs cleared their infection within 1 week and were resistant to reinfection. Animals that received IN immunization of MOMP-ISCOMs were partially protected, shedding fewer chlamydiae than did control mice. Altogether, the results suggested that IM delivery of MOMP-ISCOMs may be a suitable vaccine regimen potentially capable of inducing protective mucosal immunity against C. trachomatisinfection.

scholarly journals Dendritic Cells Pulsed with a Recombinant Chlamydial Major Outer Membrane Protein Antigen Elicit a CD4+ Type 2 Rather than Type 1 Immune Response That Is Not Protective

2002 ◽  
Vol 70 (3) ◽  
pp. 1097-1105 ◽  
Author(s):  
Jennifer Shaw ◽  
Vernon Grund ◽  
Luke Durling ◽  
Debbie Crane ◽  
Harlan D. Caldwell
Keyword(s):  
Immune Response ◽  
Dendritic Cells ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Ex Vivo ◽  
Major Outer Membrane Protein ◽  
Immunological Properties ◽  
Pulsed Dc

ABSTRACT Chlamydia trachomatis is an obligate intracellular bacterium that infects the oculogenital mucosae. C. trachomatis infection of the eye causes trachoma, the leading cause of preventable blindness. Infections of the genital mucosae are a leading cause of sexually transmitted diseases. A vaccine to prevent chlamydial infection is needed but has proven difficult to produce by using conventional vaccination approaches. Potent immunity to vaginal rechallenge in a murine model of chlamydial genital infection has been achieved only by infection or by immunization with dendritic cells (DC) pulsed ex vivo with whole inactivated organisms. Immunity generated by infection or ex vivo antigen-pulsed DC correlates with a chlamydia-specific interleukin 12 (IL-12)-dependent CD4+ Th1 immune response. Because of the potent antichlamydial immunizing properties of DC, we hypothesized that DC could be a powerful vehicle for the delivery of individual chlamydial antigens that are thought to be targets for more conventional vaccine approaches. Here, we investigated the recombinant chlamydial major outer membrane protein (rMOMP) as a target antigen. The results demonstrate that DC pulsed with rMOMP secrete IL-12 and stimulate infection-sensitized CD4+ T cells to proliferate and secrete gamma interferon. These immunological properties implied that rMOMP-pulsed DC would be potent inducers of MOMP-specific CD4+ Th1 immunity in vivo; however, we observed the opposite result. DC pulsed ex vivo with rMOMP and adoptively transferred to naive mice generated a Th2 rather than a Th1 anti-MOMP immune response, and immunized mice were not protected following infectious challenge. We conclude from these studies that the immunological properties of ex vivo pulsed DC are not necessarily predictive of the immune response generated in vivo following adoptive transfer. These findings suggest that the nature of the antigen used to pulse DC ex vivo influences the Th1-Th2 balance of the immune response in vivo.

scholarly journals Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12.

1980 ◽  
Vol 77 (8) ◽  
pp. 4592-4596 ◽  
Author(s):  
R. Chen ◽  
W. Schmidmayr ◽  
C. Kramer ◽  
U. Chen-Schmeisser ◽  
U. Henning
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Primary Structure ◽  
Major Outer Membrane Protein ◽  
Ompa Protein ◽  
K 12
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