Immunogenic and Protective Properties of Neisseria meningitidis IgA1 Protease and of Its Truncated Fragments

Zinchenko, Anatoly; Kotel’nikova, O. V.; Гордеева, Е. А.; Prokopenko, Yu. A.; Razgulyaeva, O. A.; Serova, O. V.; Melikhova, T. D.; Nokel, E. A.; Zhigis, L. S.; Zueva, V. S.; Alliluev, A. P.; Румш, Л. Д.

doi:10.1134/s1068162018010193

Cited by 6 publications

(6 citation statements)

References 19 publications

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“…For convenience of purification on metal-chelate sorbents, all recombinant proteins contained C-terminal LEH 6 sequence. The purity of the obtained compounds according to SDS gel electrophoresis data was ≥93% [1,3].…”

Section: Methodsmentioning

confidence: 99%

“…We used sera from people with bacteriologically verified meningitis caused by Nmn (13 sera), Spn (19 sera), and with meningitis of non-bacterial origin (7 sera) obtained from the 2 nd Moscow City Clinical Infectious Diseases Hospital; sera from healthy donors (20 sera) from diagnostic centers in Moscow; serum from animals after single and double infection with a sublethal dose of virulent strains Nmn, Spn, and Hib (recovered mice); sera from animals immunized with the investigated proteins [1,3].…”

Section: Methodsmentioning

confidence: 99%

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Correction to: Specific Antibodies to the Fragments of Meningococcal IgA1 Protease during the Formation of Immunity to Bacterial Infections

et al. 2022

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The features of individual fragments of IgA1 protease of Neisseria meningitidis serogroup B during the formation of immunity to bacterial infections in animals and humans were studied. The antibodies to the immunogenic regions of the studied proteins are also detected in mice infected with some bacterial pathogens and in humans with bacterial meningitis. A region of IgA1 protease was identified that is not capable of producing antibodies during immunization of animals, but that detects homologous antibodies in the blood of humans and animals recovered from bacterial infections. It has been suggested that this fragment plays a regulatory role in the process of immunogenesis.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Correction to: Specific Antibodies to the Fragments of Meningococcal IgA1 Protease during the Formation of Immunity to Bacterial Infections

et al. 2022

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“…Experimental confirmation of the protective activity of IgA1 protease is shown in a small number of works. In a series of works [64][65][66][67][68][69][70][71][72][73][74] in animal experiments, it was shown that native IgA1 protease isolated from a live virulent culture of N. meningitidis serogroup A, as well as recombinant IgA1 proteases of N. meningitidis serogroup B in active or mutant forms, and some truncated analogs of these proteins have high immunogenic and protective activity.…”

Section: Iga1 Protease and Its Fragments As A Basis For The Creation Of Therapeutic And Preventive Agentsmentioning

confidence: 99%

“…On the example of individual low-molecularweight fragments of IgA1 protease, an important role of B and T epitopes located in the N-terminal region of IgA1 protease of N. meningitidis serogroup B (strain H44/76) for the preservation of immunogenic and protective properties was demonstrated [64,65]. These proteins protected mice from infection with a live virulent culture of meningococci of the main epidemic serogroups (A, B, and C) and had the characteristic ability of proteins to form immunological memory [68,69,73].…”

Section: Iga1 Protease and Its Fragments As A Basis For The Creation Of Therapeutic And Preventive Agentsmentioning

confidence: 99%

IgA1 Protease as a Vaccine Basis for Prevention of Bacterial Meningitis

et al. 2021

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The review covers the study of the protective properties of IgA1 protease and the possibility of creating a vaccine preparation for the prevention of bacterial meningitis of various origins on its basis. Bacterial meningitis belongs to the group of socially dangerous diseases and is characterized by a severe course, numerous complications and high mortality. The approaches used at present in world practice to create antimicrobial vaccines are based on a narrow targeting against a specific pathogen. The development of a monocomponent vaccine against a wide range of bacterial pathogens with a common virulence factor is still relevant. IgA1 protease, a protein that is one of the main virulence factors of a number of gram-negative and gram-positive bacteria, can serve as such an antigen. Bacterial IgA1 protease is uniquely specific for immunoglobulins A1 (IgA1), cleaving peptide bonds in the hinge regions of the IgA1 in humans and other higher primates. Bacteria, getting on the mucous membrane, destroy IgA1, which acts as the first barrier to protect the body from infections. Neutralization of IgA1 protease at this stage can become an obstacle to the development of infection, hindering the adhesion of a number of pathogens that produce this protein. The data available in the literature on the mechanism of antibacterial protection are scattered and ambiguous. The review considers the literature data and the results of our own experiments on the protective activity of IgA1 protease. We have shown that the recombinant meningococcal IgA1 protease and some of its fragments protect mice from infection with a live virulent culture not only of meningococci of the main epidemic serogroups (A, B, C, and W135), but also of some of the most common virulent pneumococcal serotypes. The data obtained indicate the possibility of creating a monocomponent vaccine against these and, possibly, other bacterial infections. Currently, significant progress has been made in studying the structure and functions of secreted proteins in the bacteria Neisseria meningitidis and Haemophilus influenzae. In this review we describe protein translocation systems of N. meningitidis, which are related to the secretion of proteins in these bacteria, and also present modern data on the functions of these proteins. Analysis of experimental data on the structure of IgA1 protease of N. meningitidis and the formation of immunity during vaccination is of key importance in the development of prophylactic preparations.

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“…In addition, it was found [ 13 , 14 ] that some fragments of the mature enzyme also have immunogenic and protective properties against meningococcal infection. It has also been shown [ 15 ] that antibodies formed upon immunization of animals with a mature IgA1 protease are able to bind not only with the secreted protein but also with the surface of meningococcal microbial cells.…”

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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Immunogenic and Protective Properties of Neisseria meningitidis IgA1 Protease and of Its Truncated Fragments

Cited by 6 publications

References 19 publications

Correction to: Specific Antibodies to the Fragments of Meningococcal IgA1 Protease during the Formation of Immunity to Bacterial Infections

Correction to: Specific Antibodies to the Fragments of Meningococcal IgA1 Protease during the Formation of Immunity to Bacterial Infections

IgA1 Protease as a Vaccine Basis for Prevention of Bacterial Meningitis

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

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