Acid stress upregulated outer membrane proteins in clinical isolates ofNeisseria gonorrhoeae, but not most commensalNeisseria

2001 ◽  
Vol 47 (9) ◽  
pp. 871-876 ◽  
Author(s):  
R K Pettit ◽  
T M Whelan ◽  
K S Woo
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Neisseria Gonorrhoeae ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Outer Membrane Proteins ◽  
Acid Stress ◽  
Immune Serum ◽  
Gonococcal Infection ◽  
Membrane Components

Human immune serum recognition of outer membrane components from commensal and pathogenic Neisseria cultured under neutral and acidic conditions was investigated. Acid stress caused no detectable alterations in lipooligosaccharide migration and (or) staining, in outer membrane protein profiles, or in immune serum recognition of outer membrane components from Neisseria mucosa or Neisseria sicca. There was also no difference in the lipoologosaccharide electrophoretic pattern of acid- and neutral-grown Neisseria lactamica, but there were differences in outer membrane protein expression. The outer membrane protein alterations induced by acid stress in N. lactamica were not the same as those seen in isolates from patients with uncomplicated gonococcal infection, pelvic inflammatory disease, and disseminated gonococcal infection. Many differences were detected in the immune serum recognition of outer membrane components from acid- and neutral-cultured N. lactamica and from the clinical isolates of Neisseria gonorrhoeae, and these should be considered in vaccine design.Key words: Neisseria gonorrhoeae, commensal Neisseria, acid stress, outer membrane proteins.

scholarly journals Cross-linking analysis of the outer membrane proteins of Neisseria gonorrhoeae

1980 ◽  
Vol 28 (3) ◽  
pp. 785-791 ◽  
Author(s):  
W J Newhall ◽  
W D Sawyer ◽  
R A Haak
Keyword(s):  
Molecular Weight ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Neisseria Gonorrhoeae ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Outer Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cross Linking ◽  
Protein Aggregate

The organization of outer membrane proteins of Neisseria gonorrhoeae was investigated by using two-dimensional dodecyl sulfate-polyacrylamide gel electrophoresis and cross-linking agents. A naturally occurring protein aggregate, which may be composed of two proteins of 50,000 molecular weight, was detected in all strains. Treatment of whole cells with cross-linking agents yielded several additional complexes, suggesting that other proteins are arranged in the outer membrane as near neighbors. The principal outer membrane protein (molecular weight, 34,000) cross-linked (i) to itself to form a complex whch appeared to be trimeric, (ii) to the 28,000-molecular-weight outer membrane protein to form a bimolecular comlex, and (iii) to the 28,000-molecular-weight outer membrane protein in a 3:1 ratio. The formation of these complexes was independent of (i) colony type, (ii) colony opacity, (iii) pH during growth, and (iv) presence of markers for drug resistance or hypersensitivity.

scholarly journals Immunoglobulin G antibodies directed against protein III block killing of serum-resistant Neisseria gonorrhoeae by immune serum.

1986 ◽  
Vol 164 (5) ◽  
pp. 1735-1748 ◽  
Author(s):  
P A Rice ◽  
H E Vayo ◽  
M R Tam ◽  
M S Blake
Keyword(s):  
Membrane Protein ◽  
Neisseria Gonorrhoeae ◽  
Human Serum ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Immune Serum ◽  
Igg Antibodies ◽  
Porin Protein ◽  
Blocking Activity ◽  
Normal Human

Neisseria gonorrhoeae that resist complement-dependent killing by normal human serum (NHS) are sometimes killed by immune convalescent serum from patients recovering from disseminated gonococcal infection (DGI). In these studies, killing by immune serum was prevented or blocked by IgG isolated from NHS. Purified human IgG antibodies directed against gonococcal protein III, an antigenically conserved outer membrane protein, contained most of the blocking activity in IgG. Antibodies specific for gonococcal porin (protein I), the major outer membrane protein, displayed no blocking function. In separate experiments, immune convalescent DGI serum which did not exhibit bactericidal activity was restored to killing by selective depletion of protein III antibodies by immunoabsorption. These studies indicate that protein III antibodies in normal and immune human serum play a role in serum resistance of N. gonorrhoeae.

Outer Membrane Protein Composition in Disease Isolates of Haemophilus influenzae : Pathogenic and Epidemiological Implications

1980 ◽  
Vol 30 (3) ◽  
pp. 709-717
Author(s):  
Marilyn R. Loeb ◽  
David H. Smith
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Haemophilus Influenzae ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Outer Membrane Proteins ◽  
Protein Composition ◽  
The Other ◽  
Major Protein ◽  
Single Strain

The outer membrane protein composition of 50 disease isolates of Haemophilus influenzae has been determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. All strains, including 28 strains of serotype b , one strain each of serotypes a, c, d, e , and f , and 17 untypable strains, had an outer membrane protein composition typical of gram-negative bacteria, i.e., these membranes contained two to three dozen proteins with four to six proteins accounting for most of their protein content. Variation in the mobility of these major outer membrane proteins from strain to strain was common but not universal; the observed patterns provided useful data and new insight into the epidemiology of type b disease. The basic findings can be summarized as follows: (i) All 50 strains possessed three proteins (one minor and two major) each having identical mobilities. The other proteins, both major and minor, varied in mobility. (ii) All type b strains possessed a fourth (major) protein of identical mobility. (iii) The 28 type b strains, on the basis of the mobility of the six major outer membrane proteins, could be divided into eight subtypes. Of all the other strains examined, both typable and untypable, only the serotype a strain belonged to one of these subtypes. (iv) The untypable strains showed considerable variation in the mobilities of their major outer membrane proteins. Of these 17 strains, 13 had an additional major outer membrane protein not present in encapsulated strains. (v) The outer membrane protein composition of a single strain remained unchanged after many passages on solid media, but varied with the growth phase. (vi) The outer membrane protein composition of isolates obtained from nine patients during an epidemic of type b meningitis varied, indicating that a single strain was not responsible for the epidemic. At least five different strains were responsible for these nine cases. (vii) Identical outer membrane protein compositions were observed in the following: in a type b strain and a mutant of this strain deficient in capsule production, indicating that the level of capsule synthesis is not obviously related to outer membrane protein composition; in type b strains isolated from different anatomic sites of patients acutely ill with meningitis, indicating that the strain associated with bacteremia is the same as that isolated from the cerebrospinal fluid; in type b strains isolated from siblings who contracted meningitis at about the same time, indicating infection with the same strain; and in type b strains isolated from the initial and repeat infection of a single patient, suggesting that reinfection was due to the same strain.

scholarly journals Characterization of Outer Membrane Proteins in Chlamydia trachomatis LGV Serovar L2

2001 ◽  
Vol 183 (8) ◽  
pp. 2686-2690 ◽  
Author(s):  
Regina J. Tanzer ◽  
Thomas P. Hatch
Keyword(s):  
Chlamydia Trachomatis ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Outer Membrane Proteins ◽  
Major Outer Membrane Protein ◽  
Developmental Cycle ◽  
Reading Frame

ABSTRACT We used a photoactivatable, lipophilic reagent, 3′-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine, to label proteins in the outer membrane of elementary bodies ofChlamydia trachomatis LGV serovar L2 and mass spectrometry to identify the labeled proteins. The identified proteins were polymorphic outer membrane proteins E, G, and H, which were made late in the developmental cycle, the major outer membrane protein, and a mixture of 46-kDa proteins consisting of the open reading frame 623 protein and possibly a modified form of the major outer membrane protein.

scholarly journals Assembly of TolC, a Structurally Unique and Multifunctional Outer Membrane Protein of Escherichia coli K-12

2003 ◽  
Vol 185 (22) ◽  
pp. 6540-6547 ◽  
Author(s):  
John Werner ◽  
Anne Marie Augustus ◽  
Rajeev Misra
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Outer Membrane Proteins ◽  
The Other ◽  
Proteinase K ◽  
Folded Structure ◽  
K 12

ABSTRACT TolC is a multifunctional outer membrane protein of Escherichia coli that folds into a novel α-β-barrel conformation absent in the other model outer membrane proteins used in assembly studies. The data presented in this work show that the unique folded structure of TolC reflects a unique assembly pathway. During its assembly, the newly translocated nascent TolC monomers are released in the periplasm. Maturation of these nascent monomers, and possibly their oligomerization, in the periplasm precedes their insertion in the outer membrane. The completion of the assembly process is signaled by the development of a characteristic proteinase K-resistant fragment generated by cleavage at a single, periplasmically exposed, protease-sensitive site of the membrane-anchored trimer. None of the assembly steps of TolC is affected by known folding factors, such as SurA, Skp, and lipopolysaccharide, which have profound effects on the assembly of other model trimeric outer membrane proteins. Two assembly-defective TolC mutants were isolated and characterized. One of the mutants (TolCI106N) was defective in the folding of nascent monomers, while the other (TolCS350F) was impaired in steps involving trimerization and membrane insertion of folded monomers.

scholarly journals Type-specific antigens of group A Neisseria meningitidis: lipopolysaccharide and heat-modifiable outer membrane proteins

1980 ◽  
Vol 28 (2) ◽  
pp. 451-458 ◽  
Author(s):  
W D Zollinger ◽  
R E Mandrell
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Neisseria Meningitidis ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Solid Phase ◽  
Outer Membrane Proteins ◽  
Surface Antigens ◽  
Protein Antigens ◽  
Group A

The solid-phase radioimmunoassay inhibition method was used to analyze the noncapsular surface antigens of group A Neisseria meningitidis for type specificity. By use of antisera prepared against group A strains, three serologically distinct lipopolysaccharide antigens and five outer membrane protein antigens were identified among group A strains from a variety of geographical origins. Two of the lipopolysaccharide antigens were unique to group A strains while the third was similar to those on strains of other meningococcal serogroups. Fractionation of outer membrane proteins in the presence of 2% sodium deoxycholate followed by quantitative inhibition of the typing reactions with the subfractions revealed that the protein responsible for type specificity was not the principal outer membrane protein, but, most likely, the 31,000-dalton, heat-modifiable outer membrane protein. Thus, although group A strains may share a common principal outer membrane protein, typing is feasible using other surface antigens. In a survey of 82 group A strains, 93% were typable with respect to outer membrane proteins.

scholarly journals Protective Efficacy of DNA Vaccines Encoding Outer Membrane Protein A and OmpK36 ofKlebsiella pneumoniaein Mice

2010 ◽  
Vol 18 (1) ◽  
pp. 82-88 ◽  
Author(s):  
Prathiba Kurupati ◽  
N. P. Ramachandran ◽  
Chit Laa Poh
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Dna Vaccines ◽  
Outer Membrane Proteins ◽  
Protein A ◽  
Interleukin 12 ◽  
Th2 Response ◽  
Outer Membrane Protein A

ABSTRACTThe immunogenicity of DNA vaccines expressing outer membrane proteins as antigens was evaluated in this study. DNA vaccines consisting of vector pVAX1 expressing either outer membrane protein A or OmpK36 were injected into mice by either the intradermal or the intramuscular route. Antibodies elicited were shown to be specifically reactive to OmpA and OmpK36 by immunoblotting. The immunoglobulin G (IgG) antibodies elicited by both vaccines included IgG1, IgG2a, IgG2b, and IgG3. Immunized mice exhibited a predominance of IgG1 over IgG2a, therefore indicating a stronger humoral response. Mice receiving either of the DNA vaccines produced high levels of interleukin-12 (IL-12) and IL-10 and low levels of gamma interferon, suggesting the induction of a mixed Th1 and Th2 response. Sera from DNA vaccine-immunized mice had significantly higher opsonic activity in opsonophagocytic assays than did sera from the control mice. The level of protection afforded by pOmpK36 DNA injected intradermally into mice was the highest. These results suggest that both OmpA and OmpK36 are excellent candidates for use in future studies of vaccination against infections caused byKlebsiella pneumoniae. This is the first study which established the efficacy of protection afforded by DNA vaccines based on outer membrane proteins againstK. pneumoniaeinfections.

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