Literature summary for 3.4.24.13 extracted from

Kotelnikova, O.; Alliluev, A.; Zinchenko, A.; Zhigis, L.; Prokopenko, Y.; Nokel, E.; Razgulyaeva, O.; Zueva, V.; Tokarskaya, M.; Yastrebova, N.; Gordeeva, E.; Melikhova, T.; Kaliberda, E.; Rumsh, L.
Protective potency of recombinant meningococcal IgA1 protease and its structural derivatives upon animal invasion with meningococcal and pneumococcal infections (2019), Microbes Infect., 21, 336-340 .

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Application

Application	Comment	Organism
medicine	immunization of animals with IgA1pr MA28-P1004LEH6 or proteins I, II, III provides the formation of immunological memory and can protect against both meningococcal and a number of pneumococcal fatal infections. Protective properties of meningococcal IgA1pr MA28-P1004LEH6 and proteins I, II, III against pneumococci may be attributed to their conformational epitopes close in structure to epitopes of pneumococcal surface proteins. In the model of passive animal protection, sera from rabbits immunized with Streptococcus pneumoniae of different serotypes are shown to be capable of animal protection from infection with Neisseria meningitidis, at least serogroup B. Pneumococcal and meningococcal infections can cause a crossprotective effect. This makes meningococcal IgA1 proteases and their recombinant derivatives the potential components of polyvalent vaccines	Neisseria meningitidis serogroup B

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of tagged IgA1 protease of Neisseria meningitidis or several structural derivatives thereof, recombinant IgA1pr from Neisseria meningitidis serogroup B strain B44/76 with the primary structure MA28-P1004LEH6 and its N-terminal fragment (protein I, ME135-H328LEH6), proteins II and III are fusion recombinant proteins containing three or two fragments from different regions of base molecule IgA1pr MA28-P1004LEH6. Protein II contains fragments from the N-terminal, central, and C-terminal regions of the base molecule MA28-P1004LEH6, protein III contains fragments from the N-terminal and C-terminal regions of the base molecule	Neisseria meningitidis serogroup B

Cloned (Comment)

Organism

recombinant expression of tagged IgA1 protease of Neisseria meningitidis or several structural derivatives thereof, recombinant IgA1pr from Neisseria meningitidis serogroup B strain B44/76 with the primary structure MA28-P1004LEH6 and its N-terminal fragment (protein I, ME135-H328LEH6), proteins II and III are fusion recombinant proteins containing three or two fragments from different regions of base molecule IgA1pr MA28-P1004LEH6. Protein II contains fragments from the N-terminal, central, and C-terminal regions of the base molecule MA28-P1004LEH6, protein III contains fragments from the N-terminal and C-terminal regions of the base molecule

Neisseria meningitidis serogroup B

Organism

Organism	UniProt	Comment	Textmining
Neisseria meningitidis serogroup B	-	-	-
Neisseria meningitidis serogroup B B44/76	-	-	-

Synonyms

Synonyms	Comment	Organism
IgA1 protease	-	Neisseria meningitidis serogroup B
IgA1-protease	-	Neisseria meningitidis serogroup B
IgA1pr	-	Neisseria meningitidis serogroup B

General Information

General Information	Comment	Organism
additional information	immunization of mice with recombinant IgA1 protease of Neisseria meningitidis or several structural derivatives thereof protects the animals infected with a variety of deadly pathogens, including Neissseria meningitidis serogroups A, B, and C and 3 serotypes of Streptococcus pneumonia. In sera of rabbits immunized with inactivated pneumococcal cultures, antibodies binding IgA1-protease from Neisseria meningitidis serogroup B are detected. Cross-reactive protection against meningococcal and pneumococcal infections in vivo	Neisseria meningitidis serogroup B