Isolation and determination of the activity of IgA1 protease from Neisseria meningitidis

Yagudaeva, E. Yu.; Zhigis, L. S.; Razgulyaeva, O. A.; Zueva, V. S.; Melnikov, Edward E.; Zubov, V.P.; Козлов, Л. В.; Бичучер, А. М.; Kotel’nikova, O. V.; Alliluev, A. P.; Аваков, А Э; Румш, Л. Д.

doi:10.1134/s1068162010010085

Cited by 8 publications

(2 citation statements)

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“…Previous studies that identified ribosomal proteins attributed them to cytoplasmic contamination; however, in this study, with the chosen methodology, only surface-located proteins were likely to be isolated: surface locations of ribosomal proteins have been found for other bacteria (Bøhle et al , 2011; Severin et al , 2007). The remainder of the proteins identified by CSIP-MS were mostly proteins predicted to be surface located and 62 % have already been investigated as potential meningococcal vaccine targets (Wright et al , 2002; Iagudaeva et al , 2010; Granoff, 2010; Gupta et al , 2010; Hung et al , 2013). We have previously reported identifying many of these proteins by Western blot studies of whole meningococcal cell lysates (Mendum et al , 2009).…”

Section: Resultsmentioning

confidence: 99%

Identification of the immunoproteome of the meningococcus by cell surface immunoprecipitation and MS

et al. 2014

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Most healthy adults are protected from meningococcal disease by the presence of naturally acquired anti-meningococcal antibodies; however, the identity of the target antigens of this protective immunity remains unclear, particularly for protection against serogroup B disease. To identify the protein targets of natural protective immunity we developed an immunoprecipitation and proteomics approach to define the immunoproteome of the meningococcus. Sera from 10 healthy individuals showing serum bactericidal activity against both a meningococcal C strain (L91543) and the B strain MC58, together with commercially available pooled human sera, were used as probe antisera. Immunoprecipitation was performed with each serum sample and live cells from both meningococcal strains. Immunoprecipitated proteins were identified by MS. Analysis of the immunoproteome from each serum demonstrated both pan-reactive antigens that were recognized by most sera as well as subject-specific antigens. Most antigens were found in both meningococcal strains, but a few were strain-specific. Many of the immunoprecipitated proteins have been characterized previously as surface antigens, including adhesins and proteases, several of which have been recognized as vaccine candidate antigens, e.g. factor H-binding protein, NadA and neisserial heparin-binding antigen. The data demonstrate clearly the presence of meningococcal antibodies in healthy individuals with no history of meningococcal infection and a wide diversity of immune responses. The identification of the immunoreactive proteins of the meningococcus provides a basis for understanding the role of each antigen in the natural immunity associated with carriage and may help to design vaccination strategies.

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Section: Resultsmentioning

confidence: 99%

Identification of the immunoproteome of the meningococcus by cell surface immunoprecipitation and MS

et al. 2014

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“…Our team has shown [ 11 , 12 ] that mature IgA1 protease from a live culture of N. meningitidis serogroup A, recombinant variants of the enzyme from meningococcus serogroup B strain H44/76 as well as its mutants of the serine residue of the active center protected mice from infection with virulent culture of meningococci of serogroups A, B and C.…”

Section: Introductionmentioning

confidence: 99%

Highly Similar Sequences of Mature IgA1 Proteases from Neisseria meningitidis, Neisseria gonorrhoeae and Haemophilus influenzae

Karlinsky¹,

Prokopenko²,

Zinchenko³

et al. 2022

Pathogens

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The mature serine-type IgA1 protease from Neisseria meningitidis serogroup B strain H44/76 (IgA1pr1_28–1004) is considered here as the basis for creating a candidate vaccine against meningococcal meningitis. In this work, we examine the primary structure similarity of IgA1 proteases from various strains of a number of Gram-negative bacteria (N. meningitidis, Neisseria gonorrhoeae, Haemophilus influenzae) in order to find a structural groundwork for creating a broad-spectrum vaccine based on fragments of this enzyme. BLAST has shown high similarity between the primary structure of IgA1pr1_28–1004 and hypothetical sequences of mature IgA1 proteases from N. meningitidis (in 1060 out of 1061 examined strains), N. gonorrhoeae (in all 602 examined strains) and H. influenzae (in no less than 137 out of 521 examined strains). For these enzymes, common regions of sequence correspond to IgA1pr1_28–1004 fragments 28–84, 146–193, 253–539, 567–628, 639–795 and 811–1004, with identity of at least 85%. We believe that these fragments can be used in the development of a vaccine to prevent diseases caused by pathogenic strains of N. meningitidis and N. gonorrhoeae as well as a significant number of strains of H. influenzae.

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Serological Analysis of Immunogenic Properties of Recombinant Meningococcus IgA1 Protease-Based Proteins

et al. 2016

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Using the genome sequence of IgA1 protease of N. meningitidis of serogroup B, four recombinant proteins of different structure and molecular weight were constructed. These proteins were equal in inducing the formation of specific antibodies to IgA1 protease and had protective properties against meningococci. In the sera of immunized mice, anti-IgA1 protease antibodies were detected by whole-cell ELISA, which indicated the presence of IgA1 protease on the surface of these bacteria. We hypothesized that the protective properties of IgA1 protease-based antigens and IgA1 protease analogs could be realized not only via impairment of bacterium adhesion to the mucosa, but also via suppression of this pathogen in the organism. The presented findings seem promising for using these proteins as the basis for anti-meningococcus vaccine.

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Isolation and determination of the activity of IgA1 protease from Neisseria meningitidis

Cited by 8 publications

References 11 publications

Identification of the immunoproteome of the meningococcus by cell surface immunoprecipitation and MS

Identification of the immunoproteome of the meningococcus by cell surface immunoprecipitation and MS

Highly Similar Sequences of Mature IgA1 Proteases from Neisseria meningitidis, Neisseria gonorrhoeae and Haemophilus influenzae

Serological Analysis of Immunogenic Properties of Recombinant Meningococcus IgA1 Protease-Based Proteins

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