Antibody response against outer membrane components of type b strains in patients with meningitis

Vanalphen, L; Riemens, T; Zanen, H. C.

doi:10.1016/0378-1097(83)90325-7

Cited by 14 publications

(17 citation statements)

References 7 publications

(10 reference statements)

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“…It has been suggested that anticapsular antibody alone is probably not sufficient to explain natural immunity to Hib (17). However, most investigators have found (as we did) that OMP antibody is universally detectable in the acute-phase sera of patients with Hib disease and concluded that it is not protective (4,37). In a previous study, it was found by Western blotting that significantly more controls than patients had antibody directed against an OMP of 40 kDa (8).…”

Section: Discussioncontrasting

confidence: 44%

Antibodies to Haemophilus influenzae type b outer membrane proteins in children with epiglottitis or meningitis and in healthy controls

1993

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The two most common manifestations of Haemophilus influenzae type b (Hib) infection in Western communities are meningitis and epiglottitis. The role of antibodies against outer membrane proteins (OMP) in the pathogenesis of these diseases was investigated by Western blotting (immunoblotting) with an OMP antigen prepared from a local Hib strain. Acuteand convalescent-phase serum samples from 25 children with epiglottitis and 20 with meningitis and single serum samples from 19 control children in the same age group were tested. Western blots were evaluated quantitatively by use of graphs generated from a densitometer. OMP antibody was detected in all sera from patients and controls. There was no significant difference between the mean antibody level in acute-phase sera from children with meningitis (336 + 143 arbitrary units) and those from children with epiglottitis (286 + 134 arbitrary units). However, the mean OMP antibody level in sera from healthy controls, with no known history of Hib disease, was significantly higher than that in sera from patients with Hib disease within 2 days of admission to the hospital (patients [n = 35], 282 + 144; controls [n = 19], 425 236; P = 0.007). The difference was due mainly to higher levels, in control sera, of antibody against four proteins, one of which is either P1 or a comigrating protein of 49 kDa. The finding of higher levels of OMP antibody in healthy controls suggests a protective role for antibodies directed against one or more OMP. This information could be exploited in future vaccine development.

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Section: Discussioncontrasting

confidence: 44%

Antibodies to Haemophilus influenzae type b outer membrane proteins in children with epiglottitis or meningitis and in healthy controls

1993

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“…Genes encoding the porin proteins of other bacterial species, including Chlamydia trachomatis (3,41), Neisseria gonorrhoeae (6,11), Pseudomonas aeruginosa (46), and Salmonella typhi (2), have been cloned and expressed in E. coli, thus providing the opportunity for detailed molecular biological investigation of the structure and function of the products of these aopF IWRNlLAVIVPALLVAGTANAAEIYNKDGNKVDLYGK--AVGLHYfSKGNGENSYGGNXMTY--ARLGFKGETOINSDLTGYGOWEY ---NFOGNNSE-GAAQTGNKT-RLAFAGL--K--YADVGSFDYGRNYGV particular genes. Similarly, information about the P2 porin protein of Hib has only recently begun to accumulate (14,15,18,26,27,33,(42)(43)(44)(45), and the fact that this protein can be a target for antibodies protective against experimental Hib disease (33) underscores the importance of elucidating its immunogenic, antigenic, and functional properties. Cloning of the gene encoding the Hib P2 protein (18) made possible the exact determination of the amino acid sequence of this protein.…”

Section: Discussionmentioning

confidence: 99%

Primary structure of the porin protein of Haemophilus influenzae type b determined by nucleotide sequence analysis

et al. 1989

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Sequencing techniques for singleand double-stranded DNA were used to determine the nucleotide sequence of the gene encoding P2, the major outer membrane (porin) protein of Haemophilus influenzae type b (Hib).The open reading frame encoding the P2 protein comprised 361 amino acid codons. Comparison of the inferred amino acid sequence with data obtained by amino acid sequencing of the N terminus of the mature or fully processed P2 protein revealed that this protein has a signal peptide composed of 20 amino acids. N-terminal amino acid sequencing of tryptic peptides derived from purified P2 allowed direct identification of 158 of the 341 amino acids in the fully processed P2 protein; there was 100% correlation between these amino acid sequences and that inferred from the nucleotide sequence. The amino acid sequence of Hib P2 protein had 23 to 25% homology with the sequence of the OmpF porin of Escherichia coli and with that of the Neisseria gonorrhoeae porin P.IA. Codon usage in the Hib P2 gene was significantly different from that observed for a gene encoding a porin of E. coli. DNA hybridization studies indicated that there is a single copy of the P2 gene in the Hib chromosome. The availability of the nucleotide and amino acid sequences for the Hib P2 protein will facilitate investigation of the antigenic characteristics and structure-function relationship of this porin. 1100 on August 1, 2020 by guest

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“…Serum was adsorbed by the method of van Alphen et al (25). H. influenzae grown in brain heart infusion broth were harvested by centrifugation.…”

Section: Methodsmentioning

confidence: 99%

Antigenic drift of Haemophilus influenzae in patients with chronic obstructive pulmonary disease

et al. 1989

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Differences in the major outer membrane protein b,c (molecular weight, 39,000 to 41,000) of related Haemophilus influenzae strains isolated from the sputum of patients with chronic obstructive pulmonary disease were analyzed biochemically and immunologically. Protein b,c was isolated from a total of six related H. influenzae strains from two chronic obstructive pulmonary disease patients. After CNBr digestion of the proteins, the differences in size appeared in the larger of the two fragments. Trypsin and chymotrypsin digests of proteins from related H. influenzae strains showed that proteins differed by only a few peptides or were very similar, in contrast to the peptide maps of proteins from nonrelated strains. Peptide analysis of b,c proteins from related H. influenzae strains by high-performance liquid chromatography after Staphylococcus aureus V8 protease digestion and amino acid analysis of corresponding fractions revealed highly comparable patterns, indicating only minor differences in the amino acid sequences of these proteins. Immunization of rabbits with intact bacteria of four related H. influenzae strains resulted in a strong anti-protein b,c antibody response in all animals. In three of four rabbits, antibodies specific for the b,c protein of the strain used for immunization were elicited, indicating that the changed proteins contained specific immunodominant epitopes. Anti-protein b,c antibodies promoted strain-specific, complement-dependent, bactericidal activity. From these results, we conclude that H. influenzae shows antigenic drift in immunodominant epitopes, caused by small changes in amino acid composition of the b,c protein. Antibodies to these epitopes promote complement-dependent bactericidal activity.

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Antibody response against outer membrane components of type b strains in patients with meningitis

Cited by 14 publications

References 7 publications

Antibodies to Haemophilus influenzae type b outer membrane proteins in children with epiglottitis or meningitis and in healthy controls

Antibodies to Haemophilus influenzae type b outer membrane proteins in children with epiglottitis or meningitis and in healthy controls

Primary structure of the porin protein of Haemophilus influenzae type b determined by nucleotide sequence analysis

Antigenic drift of Haemophilus influenzae in patients with chronic obstructive pulmonary disease

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