Biochemical characterization of glucosaminylmuramyldipeptide binding sites of murine macrophages

AbstractBy using radioligand analysis, murine peritoneal macrophages were shown to express several hundred high-affinity cell surface GMDP-binding sites (Ka 350 pM). Photoaffinity labeling followed by SDS-PAGE enabled us to identify 32–34 and 38 kDa proteins inside these cells that bound GMDP specifically

Mechanisms of defense formation against meningococcal infection in mice immunized with synthetic peptides

Immunization of mice with synthetic peptide fragments of conservative sites of meningococcal outer membrane proteins led to defense formation against infection with virulent serogroup A and B Meningococci. The role of cellular immunity in the formation of defense against meningococcal infection after immunization with the peptides and the possibility of stimulating lymphocyte population with these peptides were demonstrated. © Springer Science+Business Media, Inc. 2007

Mechanisms of defense formation against meningococcal infection in mice immunized with synthetic peptides

Immunization of mice with synthetic peptide fragments of conservative sites of meningococcal outer membrane proteins led to defense formation against infection with virulent serogroup A and B Meningococci. The role of cellular immunity in the formation of defense against meningococcal infection after immunization with the peptides and the possibility of stimulating lymphocyte population with these peptides were demonstrated. © Springer Science+Business Media, Inc. 2007

Induction of Anti-Meningitis Immunity by Synthetic Peptides: II. Immunoactive Synthetic Fragments of the OpaB Protein from Neisseria meningitidis

Mice of various lines were immunized by 11 synthetic peptides that correspond to the sequences of fragments of the OpaB protein from the outer membrane of Neisseria meningitidis involving the known human T-helper epitopes and all the potential mouse T-helper epitopes calculated for the protein. The mice were immunized with the free peptides without their conjugation with a protein carrier. Most of the peptides were found to induce in mice the production of antipeptide antibodies. Mice protection against the experimental infection by a virulent strain of N. meningitidis of the B serotype was studied, and two peptides were shown to exert the most pronounced protective effect

Protective properties of synthetic peptides of outer meningococcal membrane

Peptide fragments of conservative sites of PorA, OpaB, and NspA proteins of the outer membrane of serogroup B meningococci were synthesized. These peptides caused a pronounced protective effect in immunized mice infected with virulent homologous and heterologous strains of serogroups B and A meningococci. The protective effect appreciably increased, if the studied peptides were associated in a polycomponent preparation, which can be used in the construction of meningococcal bivalent B+A vaccine. © Springer Science+Business Media, Inc. 2005

Induction of antimeningitis immunity by synthetic peptides. II. Immunoactive synthetic fragments of the OpaB protein from Neisseria meningitidis

Mice of various lines were immunized by 11 synthetic peptides that correspond to the sequences of fragments of the OpaB protein from the outer membrane of Neisseria meningitidis involving the known human T-helper epitopes and all the potential mouse T-helper epitopes calculated for the protein. The mice were immunized with the free peptides without their conjugation with a protein carrier. Most of the peptides were found to induce in mice the production of antipeptide antibodies. The mice protection against the experimental infection by a virulent strain of N. meningitidis of the B serotype was studied, and two peptides were shown to exert the most pronounced protective effect

Induction of antimeningitis immunity by the synthetic peptides. I. The immunoactive synthetic fragments of porin a from Neisseria meningitidis

Fourteen peptides corresponding to sequences of all the exposed and some of the transmembrane protein regions of porin A from the outer membrane of Neisseria meningitidis strain B:15:P1.7,16 were synthesized. Mice of various lines were immunized with the free peptides not conjugated with any protein carrier. It was shown that the majority of the peptides possess immunogenic properties. Two peptides were identified binding to antibodies present in the serum of mice after meningitis. Protective properties of a number of the synthesized peptides were studied, and three peptide sequences inducing mice protection from an experimental infection with N. meningitidis were identified