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At least 271 records · Page 15Linked to original sources
PubMed1982

Cross protection in mice with the Smith diffuse stain of Staphylococcus aureus versus a type Ia strain of group B streptococci.

Active immunization of mice with whole cell vaccine or cell surface polysaccharide from either the Smith diffuse strain of Staphylococcus aureus or SS-615 (type Ia of group G streptococci) protected against challenge by either the homologous or heterologous strains. In the peritoneal cavity of mice immunized with either of these organisms rapid phagocytosis and reduction of the viable cells was observed at 6 h after the challenge. Cell surface polysaccharides extracted from strains Smith diffuse and SS-615, both prepared by the same procedure as that of the Smith surface antigen, were capable of absorbing the protective antibody in rabbit hyperimmune sera prepared with homologous or heterologous strains.

Animals↗
PubMed1982

Cross-protection against fecal excretion of Yersinia enterocolitica and Yersinia pseudotuberculosis in mice by oral vaccination of viable cells.

Mice given orally either the O3, O9, or O5B serovar of Yersinia enterocolitica showed protection upon subsequent oral challenge with another of these strains. Excretion of serovar O3 in the feces was inhibited in mice surviving oral challenge with Yersinia pseudotuberculosis IVA. Cross-reaction of O antigen among these four strains was 32 or more times lower than the homologous titers.

Animals↗
PubMed2005

Multivalent liposome-based vaccines containing different serosubtypes of PorA protein induce cross-protective bactericidal immune responses against Neisseria meningitidis.

Four serosubtypes (P1.7, 16, P1.7-2, 4, P1.19, 15 and P1.5-1, 10-4) of the PorA outer-membrane protein of Neisseria meningitidis were purified as recombinant proteins and incorporated into liposomes to investigate their immunogenicity. Each serosubtype induced high levels of bactericidal activity against the homologous strain. In addition, liposome preparations containing multiple serosubtypes induced high levels of bactericidal activity against each of the four strains. Significantly, antisera raised against monovalent and multivalent liposomes also showed cross-reactive bactericidal activity against heterologous strains. These data demonstrate that multivalent liposome vaccines, containing multiple PorA serosubtypes, have the potential to provide protection against a broad range of meningococcal strains.

Animals↗
PubMed1974

Cross-protection between group B arboviruses: resistance in mice to Japanese B encephalitis and St. Louis encephalitis viruses induced by Dengue virus immunization.

Albino Swiss mice, immunized with any of several types and strains of dengue viruses, were afforded substantial protection against peripheral Japanese B encephalitis or St. Louis encephalitis virus challenge. Dengue-2 (New Guinea "C")-immunized mice showed, 10 and 20 weeks after immunization, undiminished resistance with concomitant cyclophosphamide treatment and virus challenge. Examination of the effects of immunization on Japanese B encephalitis virus pathogenesis, after virus challenge with concomitant cyclophosphamide treatment, indicated that protection was associated with decreased viremia and virtually no virus replication in the brain as compared with controls. These effects could be demonstrated before detection of any neutralizing antibody to the challenge virus. From the applied aspect, the data support the hypothesis, based on epidemiological evidence and experiments in hamsters, that prior exposure of man to dengue viruses can confer some degree of protection against Japanese B encephalitis or St. Louis encephalitis disease.

Animals↗
PubMed2003

Identification of a cross-reactive epitope widely present in lipopolysaccharide from enterobacteria and recognized by the cross-protective monoclonal antibody WN1 222-5.

Septic shock due to infections with Gram-negative bacteria is a severe disease with a high mortality rate. We report the identification of the antigenic determinants of an epitope that is present in enterobacterial lipopolysaccharide (LPS) and recognized by a cross-reactive monoclonal antibody (mAb WN1 222-5) regarded as a potential means of treatment. Using whole LPS and a panel of neoglycoconjugates containing purified LPS oligosaccharides obtained from Escherichia coli core types R1, R2, R3, and R4, Salmonella enterica, and the mutant strain E. coli J-5, we showed that mAb WN1 222-5 binds to the distal part of the inner core region and recognizes the structural element R1-alpha-d-Glcp-(1-->3)-[l-alpha-d-Hepp-(1-->7)]-l-alpha-d-Hepp 4P-(1-->3)-R2 (where R1 represents additional sugars of the outer core and R2 represents additional sugars of the inner core), which is common to LPS from all E. coli, Salmonella, and Shigella. WN1 222-5 binds poorly to molecules that lack the side chain heptose or lack phosphate at the branched heptose. Also molecules that are substituted with GlcpN at the side chain heptose are poorly bound. Thus, the side chain heptose and the 4-phosphate on the branched heptose are main determinants of the epitope. We have determined the binding kinetics and affinities (KD values) of the monovalent interaction of E. coli core oligosaccharides with WN1 222-5 by surface plasmon resonance and isothermal titration microcalorimetry. Affinity constants (KD values) determined by SPR were in the range of 3.6 x 10-5 to 3.2 x 10-8 m, with the highest affinity being observed for the core oligosaccharide from E. coli F576 (R2 core type) and the lowest KD values for those from E. coli J-5. Affinities of E. coli R1, R3, and R4 oligosaccharides were 5-10-fold lower, and values from the E. coli J-5 mutant were 29-fold lower than the R2 core oligosaccharide. Thus, the outer core sugars had a positive effect on binding.

Antibodies, Monoclonal↗
PubMed1996

Transferrin receptors of Neisseria meningitidis: promising candidates for a broadly cross-protective vaccine.

Production of a meningococcal vaccine capable of generating long-lasting immunity in all age groups is still a high priority worldwide. Iron-regulated outer-membrane proteins have attracted considerable attention in recent years and it has become increasingly evident that the meningococcal transferrin-binding proteins, TBP1 and TBP2, have characteristics compatible with a safe and broadly cross-reactive vaccine candidate. Both TBPs are surface-exposed and immunogenic in man and animals, and antibodies to their native structure are bactericidal to homologous and many heterologous strains. These include strains from various serogroups, serotypes and serosubtypes, with no obvious correlation between bactericidal activity and the identity of the strains or the molecular mass of the heterogeneous TBP2 molecule. A meningococcal vaccine based on, or enriched with, undenatured TBPs from one or more strains, in combination with conventional polysaccharide-based vaccines, might increase the spectrum of strains against which protection can be achieved to include serogroup B strains. In this review, the structure-function and immunological properties of TBP1 and TBP2 are discussed.

Amino Acid Sequence↗