Protective properties of recombinant igA1 protease from meningococcus

Abstract

The study of enzymatic and protective properties of recombinant IgA1 protease in active and mutant form showed that active form of IgA1 protease exhibited species – and type-specificity for mouse and human immunoglobulins. Mutant form, which did not exhibit enzymatic activity, had protective properties against meningococcal infection, induced by meningococcus serogroup A, B and C protecting the mice from lethal infection by living virulent culture of heterologous serogroups of meningococcus. Obtained results make it possible to consider IgA1 protease as a perspective preparation at the stages of development of polyvalent vaccine for protection the people from meningococcal infection of various etiology

Peculiarities of the Formation of Antimeningococcus Immunity in Mice Immunized with Fragments of N. meningitidis IgA1 Protease

“…On day 30 after a single and on day 10 after double immunization, serum titers of antibodies to IgA1pr were measured by adsorption of IgA1pr on the plates. The protective activities of the preparations were evaluated on day 12 after double immunization as described previously [2].…”

“…Many authors suggest that IgA1 proteases (IgA1pr), important factors of bacterial virulence, can be used for protection from these pathogens [8,9]. We have shown in animal experiments that recombinant IgA1pr in active and mutant forms and some short analogs of meningococcal IgA1pr are characterized by high immunogenic and protective activities and protect mice from infection with live virulent culture of meningococci of the main epidemic serogroups (A, B, and C); they also exhibit capacity typical of proteins to the formation of immunological memory [2,4,12].…”

A new methodological approach to estimation of IgA1 and IgA2 content in human serum using recombinant IgA1 protease from Neisseria meningitidis

“…The enzymatically active and inactive (with replacement of Ser 267 by Ala) forms of recombinant IgA1 protease from N. meningitidis of serogroup B strain H44/76 (further AE9 and SA4, respectively) with molecular weight of about 107 kDa were obtained and used for preparation of sensitized plates as described in previous publications (Kotel'nikova et al 2013;Rumsh et al 2011). 96-well polystyrene plates with flat bottom, lyophilized human immunoglobulins IgA, IgA1, and IgG (Fitzgerald, USA), horseradish peroxidase-conjugated goat antibody to human IgA, IgA1, and IgG (Biosciences Pharmingen USA) were used as received.…”

“…All measurements for each IgA1 protease form were performed in triplicate. The IgA1 titer was determined by subtraction of absorbance values obtained by titration with active IgA1 (AE9) protease from the values obtained with inactive (SA4) IgA1 protease as described earlier (Kotel'nikova et al 2013). The data were processed using MS Office Excel software.…”

“…The enzymatic activity of IgA1 protease was assayed using human IgA1 and IgG by SDS-PAGE as described earlier (Kotel'nikova et al 2013).…”