Effects of proteolytic enzymes on the outer membrane proteins of Neisseria gonorrhoeae

Blake, M. S.; Gotschlich, Emil C.; Swanson, John

doi:10.1128/iai.33.1.212-222.1981

Cited by 79 publications

(58 citation statements)

References 20 publications

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“…PIII is resistant to proteases in the intact gonococcus or in isolated OM blebs (55), which, by electron microscopy, appear to be sealed vesicles . However, the purified protein is very readily attacked by proteases (31).…”

Section: Discussionmentioning

confidence: 96%

The DNA sequence of the structural gene of gonococcal protein III and the flanking region containing a repetitive sequence. Homology of protein III with enterobacterial OmpA proteins.

Gotschlich¹,

Seiff²,

Blake³

1987

The Journal of Experimental Medicine

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The insert of a lambda gt11 clone expressing gonococcal protein III was sequenced. The deduced amino acid sequence showed a coding frame of 236 amino acids with a typical 22-amino-acid signal peptide, followed by the known NH2-terminal sequence of PIII. The mature protein has a molecular weight of 23,298. It was found that PIII had extensive and very striking homology to the carboxy-terminal portion of enterobacterial OmpA proteins. The homology encompasses the OmpA domain that is believed to be located in the periplasmic space. If the disposition of PIII across the OM is analogous, then the surface-exposed domain consists of less than 40 amino acids. These include a potential 15-amino-acid disulfide loop, a feature not found in OmpA proteins. Hybridization studies with the sequenced insert indicated that it contained a repetitive sequence that occurred at least 20 times in the genome. By additional hybridization studies the area containing the repetitive sequence was narrowed to a region of 43 bp. This region contained an exact copy of the consensus sequence of a 26-bp repetitive sequence recently described. An analogous sequence recurs in an inverted orientation 53 bp downstream.

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Section: Discussionmentioning

confidence: 96%

The DNA sequence of the structural gene of gonococcal protein III and the flanking region containing a repetitive sequence. Homology of protein III with enterobacterial OmpA proteins.

Gotschlich¹,

Seiff²,

Blake³

1987

The Journal of Experimental Medicine

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“…B. Comparison of deduced amino acid sequences of OpaA and OpaB proteins from Bhat et al (1991). Opa and Por (the Ng outer membrane porin) proteins of Ng have been shown to be sensitive to trypsin (Swanson, 1978;Blake et al, 1981). The results of the limited trypsinolysis are shown in Fig.…”

Section: Fig 1 a A Schematic Diagram Of The Proposed Conformation Ofmentioning

confidence: 99%

Proteoglycan receptor binding by Neisseria gonorrhoeae MS11 is determined by the HV‐1 region of OpaA

Grant

Bos

Belland

1999

Molecular Microbiology

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SummaryThe interaction of the OpaA protein of Neisseria gonorrhoeae MS11mk with heparan sulphate-containing proteoglycan receptors on Chang conjunctiva epithelial cells was examined using isolated receptor binding and cell adherence/internalization assays. OpaA deletion proteins, in which the four surface-exposed regions of the protein were deleted individually, and chimeric OpaA/B proteins, in which the surface-exposed regions of the OpaA and OpaB proteins were exchanged, were expressed in N. gonorrhoeae. The recombinant deletion proteins and the chimeric OpaA/B proteins were surface exposed in the outer membrane of N. gonorrhoeae.

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“…Earlier data obtained from proteolytic digests of whole gonococci and of outer membrane preparations suggest that very little if any of protein III is exposed on the surface of the bacterium, as no degradation of the protein is observed when analyzed by SDS-PAGE (14). This is in complete contrast to the results obtained when the purified protein is exposed to the same endopeptidases .…”

Section: Discussionmentioning

confidence: 76%

Isolation and partial characterization of the reduction-modifiable protein of Neisseria gonorrhoeae.

Lytton¹,

Blake²

1986

The Journal of Experimental Medicine

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For several years investigators have examined and characterized some of the surface antigens of the bacterium Neisseria gonorrhoeae, including pili, lipopolysaccharide (LPS), and various proteins of the outer membrane (for review see references 1 and 2). The particular interest in our laboratory has been to understand how all of the components within the gonococcal outer membrane function to the advantage of the organism. In this effort, we have isolated and purified members of the protein I family and found them to be trimeric complexes that form voltage-dependent, anion-specific transmembrane porins (3-5). Furthermore, we have purified several members of the protein II family, one of which confers the opaque phenotype to gonococcal colonies (6) whereas another seems to be implicated in the association of gonococci with polymorphonuclear leukocytes (7). In order to complete our information about the outer membrane proteins and help us understand how these protein components of the gonococcal outer membrane might work in concert, we turned our attention to the last remaining major outer membrane protein family, the reductionmodifiable proteins, or proteins III .Protein III is present in all strains of gonococci examined to date and differs from the other surface-exposed gonococcal outer membrane proteins by its high degree of intrastrain and interstrain homology in molecular weight, structure, and immunology (8, 9). These characteristics make protein III unique among the major outer membrane antigens of the gonococcus, as proteins I and II, as well as LPS and pili, all appear to display a considerable degree of variability either within a strain or between strains (1, 2). Because it has been hypothesized that this variability was in part due to the immunologic pressure of the human host, it was puzzling that gonococci would rigidly conserve such a surface antigen. For this reason it seemed that we should isolate and purify this protein in order to study its biochemical and immunochemical nature in more detail . Thus, this article will present a newly devised method of isolating and purifying protein III and a partial characterization of the structure and immunochemistry of the molecule based on our investigations that use the purified protein . The method used for isolating protein III in large quantities is a simple refinement of the

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Effects of proteolytic enzymes on the outer membrane proteins of Neisseria gonorrhoeae

Cited by 79 publications

References 20 publications

The DNA sequence of the structural gene of gonococcal protein III and the flanking region containing a repetitive sequence. Homology of protein III with enterobacterial OmpA proteins.

The DNA sequence of the structural gene of gonococcal protein III and the flanking region containing a repetitive sequence. Homology of protein III with enterobacterial OmpA proteins.

Proteoglycan receptor binding by Neisseria gonorrhoeae MS11 is determined by the HV‐1 region of OpaA

Isolation and partial characterization of the reduction-modifiable protein of Neisseria gonorrhoeae.

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