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Immunogenic and Protective Properties of Neisseria meningitidis IgA1 Protease and of Its Truncated Fragments
Ist Teil von
Russian journal of bioorganic chemistry, 2018, Vol.44 (1), p.64-72
Ort / Verlag
Moscow: Pleiades Publishing
Erscheinungsjahr
2018
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
Four recombinant proteins, MA
28
–P
1004
LEH
6
, ME
135
–H
328
LEH
6
, MW
329
–H
622
LEH
6
and MH
835
–P
1004
LEH
6
, were prepared based on the genomic sequence of IgA1 protease from
Neisseria meningitidis
serogroup B strain H44/76. The immunogenic and protective properties of these proteins were studied in a mouse model. The predicted T- and B-epitopes located in the N-terminal part of amino acid sequence of this enzyme are very important for the formation of effective protection against meningococci of the three main epidemic serogroups A, B, and C. The small-sized recombinant protein having the sequence ME
135
–H
328
LEH
6
(molecular weight 23367 Da) appears to be as protective against meningococci of the tested serogroups as the high molecular MA
28
–P
1004
LEH
6
(molecular weight 109019 Da), the latter being a large-sized analog of full-length IgA1 protease. These proteins can be promising candidates for a polyvalent meningococcal vaccine.