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PubMed1993

Role of the S-layer proteins of Campylobacter fetus in serum-resistance and antigenic variation: a model of bacterial pathogenesis.

Campylobacter fetus are microaerophilic gram-negative bacteria that are pathogens of animals and humans. These organisms possess paracrystalline surface (S-) layers, composed of acidic high molecular weight proteins. C. fetus strains possessing S-layers are resistant to C3b binding, which explains both serum and phagocytosis-resistance. C. fetus strains also can vary the subunit protein size, crystalline structure, and antigenicity of the S-layer it expresses. Therefore, its S-layer permits C. fetus to resist complement and antibodies, two of the key defenses against extracellular pathogens. C. fetus possesses several full-length genes encoding S-layer proteins with both conserved and divergent sequences, which permits gene rearrangement and antigenic variation.

Antigenic Variation↗
PubMed1993

Regional chromosomal assignment of the Kell blood group locus (KEL) to chromosome 7q33-q35 by fluorescence in situ hybridization: evidence for the polypeptide nature of antigenic variation.

The gene encoding the Kell blood group polypeptide has been localized to chromosome 7q33-35 by in situ hybridization using a biotinylated 1.1-kb DNA fragment containing the 3' half of the human cDNA. This assignment is in accord with genetic localization using antigenic variation as a marker, and strongly suggests that Kell antigenic determinants are part of the polypeptide chain rather than the associated sugar molecules.

Antigenic Variation↗
PubMed1989

Mechanism of antigenic variation in Shigella flexneri bacilli. I. Selective lethal effect of normal sera on mixed population of S. flexneri 1b serotype and its antigenic 3b mutant.

Normal non-immune calf, human and mice sera kill-preferentially the Shigella flexneri 1b serotype cells with antigenic formula I; 3, 4, 6 leaving the antigenic mutant cells of the serotype 3b with antigenic formula III; 3, 4, 6. The strongest lethal action was observed in normal calf serum. This serum makes possible to obtain the 3b serotypes mutant from pure population of 1b serotype cells. Thermal inactivation of the complement deprives the serum of its selective activity.

Animals↗
PubMed1993

Antigenic diversity, antigenic variation and merozoite surface protein 1.

Antigenic diversity and immune evasion by the parasite are important factors in the epidemiology of malaria and in determining the incidence of severe malaria. The dynamics of the parasitaemia in current studies in mice immunized with P.c.chabaudi native MSP1 or recombinant C-terminal subunits thereof, strongly indicate evasion of components of the immune response induced by these antigens by parasites multiplying after challenge infection.

Adult↗
PubMed1984

Modification of telomeric DNA in Trypanosoma brucei; a role in antigenic variation?

Expression of surface antigen genes in Trypanosoma brucei occurs at expression sites located near telomeres. Since only one antigen is produced at a time, a mechanism must exist to prevent the simultaneous activity of multiple expression sites. Here we report that PstI and PvuII restriction sites in silent telomeric antigen genes are partially uncleavable , presumably as a consequence of DNA modification. The modification, which is absent in transcribed genes but returns after gene inactivation, may be specific for telomeric DNA because (1) it is not detected in non-telomeric genes; (2) modification is highest close to the telomere; (3) the level of modification in a telomeric gene is influenced by the size of the telomeric DNA segment downstream. Whether telomere modification is cause or consequence of antigen gene switch-off remains to be determined.

Animals↗
PubMed2006

Within-host dynamics of antigenic variation.

Genomes of some parasites contain dozens of alternative and highly diverged surface antigens, of which only a single one is expressed in any cell. Individual cells occasionally change expression of their surface antigen, allowing them to escape immune surveillance. These switches appear to occur in a partly random way, creating a diverse set of antigenic variants. In spite of this diversity, the parasitemia develops as a series of outbreaks, in which each outbreak is dominated by relatively few antigenic types. Host-specific immunity eventually clears the dominant antigenic types, and a new outbreak follows from antigenic types that have apparently been present all along at low frequency. This pattern of sequential dominance by different antigenic types remains unexplained. We review the five most prominent theories, which have developed mainly from studies of the protozoans Trypanosoma and Plasmodium, and the bacterial spirochete Borrelia. The most promising theories depend on some combination of mechanisms to create favored connectivity pathways through the matrix of transitions between variants. Favored pathways may arise from biased switches at the molecular level of gene expression or from biases imposed by immune selection. We illustrate the concept of connectivity pathways by reanalysis of data on transitions between variants from Borrelia hermsii.

Animals↗
PubMed1986

Antigenic variation among human strains of influenza C virus detected with monoclonal antibodies to gp88 glycoprotein.

Antigenic variation among influenza C virus strains was investigated with monoclonal antibodies against gp88 glycoprotein. Seven monoclonal antibodies obtained were tentatively classified into two groups, A and B. The group A antibodies had hemagglutination inhibition (HI), hemolysis inhibition and neutralization activities whereas the group B antibodies possessed none of them. A comparison of antigenicity among 15 human strains with these antibodies in radioimmunoprecipitation and HI tests showed that the regions recognized by the group A antibodies undergo considerable changes, whereas those by group B are conserved among the strains.

Animals↗
PubMed2001

Antigenic variation of gonococcal pilin expression in vivo: analysis of the strain FA1090 pilin repertoire and identification of the pilS gene copies recombining with pilE during experimental human infection.

Antigenic variation of gonococcal pilin involves a family of variable genes that undergo homologous recombination, resulting in transfer of variant sequences from the pilS silent gene copies into the complete pilE expression locus. Little is known about the specific recombination events that are involved in assembling new variant pilin genes in vivo. One approach to understanding pilin variation in vivo is to carry out experimental human infections with a gonococcal strain having a fully characterized repertoire of pilin genes, so that the specific recombination events occurring in vivo can be determined. To this end, the authors cloned, sequenced and mapped the pilin genes of strain FA1090 of Neisseria gonorrhoeae. This strain contains one pilE locus and 19 silent gene copies that are arranged in five pilS loci; the pilE locus and four of the pilS loci are clustered in a 35 kb region of the chromosome. The general features of the pilin loci in FA1090 are similar to those in strain MS11, in which the mechanism of pilin variation has been extensively studied. However, none of the silent copy sequences are identical in the two strains, which emphasizes the extreme variability in this gene family among gonococci. Three male volunteers were inoculated with the same variant of strain FA1090 and developed urethritis within 2--4 d. The pilE gene sequences from a total of 23 colonies cultured from the subjects were analysed, determining which pilS silent copy donated each portion of the expressed pilE genes. There were 12 different pilin variants, one of which was the original inoculum variant, among the in vivo-expressed pilE gene sequences. The pilE of the inoculum variant was derived entirely from a single silent copy (pilS6c1). However, the pilE genes in the majority of the colonies cultured from the infected subjects were chimeras of sequence derived from two or three silent copies. Recombination to generate new pilE sequences involved exchange of single variable minicassettes, multiple minicassettes, entire silent gene copies, or (rarely) recombination within a minicassette.

Antigenic Variation↗
PubMed1984

Studies of the antigenic variation in poliovirus type 1. Selection and analysis of variant strains with monoclonal antibodies by neutralization.

Nine neutralizing monoclonal antibodies were used in a preliminary study of the antigenic variation of poliovirus type 1. Six antigenic variants were selected and five distinct epitopes involved in neutralization were identified. Four of these epitopes are thought to be clustered within a single antigenic site. In kinetic studies, the neutralization of poliovirus by monoclonal antibodies was shown to be a single hit process.

Animals↗
PubMed1984

Antigenic variation and the structure of influenza virus glycoproteins.

Influenza is impossible to control by vaccination because of variation in the two surface antigens of the virus, the haemagglutinin (HA) and neuraminidase (NA). This variation is caused by sequence changes in the genes coding these antigens and this review summarizes recent information on the structure of the HA and NA, the way in which these glycoproteins vary and the effects of the changes on the antigenic properties of the virus.

Amino Acid Sequence↗
PubMed1975

Antigenic variation of neuraminidase of human type A influenza (H3N2) viruses isolated in Berlin (West).

After the emergence of the A/Hong Kong/1/68 (H3N2) strain of influenza virus antigenic variation of the hemagglutinin and neuraminidase antigens have been demonstrated leading to the identification of the variants A/England/42/72,a/Port Chalmers/1/73 and A/Scotland/840/74. This study describes antigenic changes of neuraminidases in influenza viruses isolated since 1968 in Berlin (West). A collection of 13 isolates of human type A influenza was studied in neuraminidase inhibition tests. The results are in line with data from other laboratories indicating a major change in the neuraminidase antigen as early as December 1969. The strains isolated at that time cross-reacted with an antiserum against the N2-Hong Kong enzyme to less than 50%. During the following years (1970 to 1972) the neuraminidase remained fairly stable. Serological cross-reactions showing 47 to 38% inhibition as compared to the homologous N2-antigen. The neuraminidase of the A/Berlin/3/72 strain revealed a close antigenic relationship to the later appearing A/Port Chalmers 1/73 variant. Two strains isolated in 1975 (January) showed an even further drift away from the then representative A/Port Chalmers/1/73 strain. The fact that the neuraminidase antigens of the Berlin viruses had changed in December 1969 may account for the severe 1969/70 influenza epidemic in Berlin affecting a large proportion of the population. Prevalent anti-neuraminidase antibodies may play a role in restricting a variant carrying a new hemagglutinin to primarily infected individuals by cross-reacting with a closely related enzyme.

Antigens, Viral↗
PubMed2002

Antigenic variation within the subunit protein of members of the colonization factor antigen I group of fimbrial proteins in human enterotoxigenic Escherichia coli.

Colonization factor antigens (CFAs) of human enterotoxigenic Escherichia coli can be divided in groups based on the N-terminal amino acid sequence of their major subunit protein. One of the groups that has been distinguished in this way, is the CFA/I group of fimbriae. The sequence of the fimbrial subunit genes in the operons encoding the antigens CS4, CS14 and CS17, all members of this group, was determined. A duplication of the fimbrial subunit gene (csuA) was found in the CS14 operon, both genes encoding very similar proteins. Purified CS14 fimbriae consist of two proteins with different molecular masses (15.5 and 17.0 kDa) but identical N-terminal amino acid sequences, which strongly suggests that both csuA genes are transcribed. A phylogenetic tree derived from the amino acid sequences of the CFA/I, CS1, CS2, CS4, CS14, CS17 and CS19 subunit proteins shows that CS1, CS17 and CS19 belong to the same subgroup. CFA/I, CS4 and CS14 belong to a second subgroup, while CS2 is distinct within the CFA/I group of fimbriae. The genetic similarity between CS1, CS17 and CS19 is reflected in the substantial immunological cross-reactivity observed, both between their protein subunits and intact fimbriae.

Agglutination Tests↗
PubMed1976

The relation of agglutinins to antigenic variation of Trypanosoma lewisi.

During the course of infection in the rat, Trypanosoma lewisi produces 2 antigenic variants: the 1st represents the initial, reproducing population of cells; and the 2nd the nonreproducing, ablastin-inhibited adult population. The specificities of the agglutinins elicited by the variants were studied by adsorption and agglutination methods and the newer immunoelectroadsorption technic. It was found that the reproducing variant has a surface antigen that reacts with the agglutinin specific for the adult variant, but this antigen does not become immunogenic until transformation to the adult variant occurs. It was also found, with fractions of immune sera obtained by gel filtration, that the agglutinin specific for the reproducing variant is IgG and that specific for the adult variant, IgM. The antigenic variants of pathogenic and nonpathogenic trypanosomes are compared, and the roles of trypanocidal and ablastic antibodies in the induction of antigenic variation are discussed.

Adsorption↗
PubMed1994

Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.

Seven antigenic variants obtained from a single field isolate of foot-and-mouth disease virus, serotype A12, differ only at residues 148 and 153 in the immunodominant loop of viral protein VP1. Synthetic peptides corresponding to the region 141-160 are highly immunogenic. UV circular dichroism shows that (i) in aqueous solution the peptides are nearly identical, but in 100% trifluoroethanol they display helix-forming properties which correlate well with their serological crossreactivities for anti-peptide sera, and (ii) these properties are insensitive to substitutions at position 153, except for proline, but are highly sensitive to substitutions at position 148. This pattern can be explained by the effects of these substitutions on the amphiphilic character and positions of helices postulated in the region 146-156. Molecular models indicate that residues 147, 148, 150, 151, 153-155, and 157 are most likely to interact with residues of the antibody paratopes. The data are consistent with the existence of an inverse gamma-turn around Pro-153, and a beta-turn at the cell-attachment site at residues 145-147.

Amino Acid Sequence↗