Isolation of an Antigenic Oligosaccharide Fraction from Leptospira interrogans serovar canicola with a Monoclonal Antibody

Ono, Etsuro; Naiki, Masaharu; Yanagawa, Ryo

doi:10.1099/00221287-130-6-1429

Cited by 15 publications

(13 citation statements)

References 15 publications

(3 reference statements)

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“…The majority were found to be localized in the LPS-like component of the cell. Ono [7], Masuzawa [8], and Schoone [9] reached similar conclusions and identified serovar-specific epitopes within the groups Canicola and Icterohaemorrhagiae.…”

Section: Introductionmentioning

confidence: 56%

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Immunodominant antigens recognized by the human immune response to infection by organisms of the species Leptospira interrogans serogroup Australis

Cinco¹

1992

FEMS Microbiology Letters

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SUMMARYSerum samples from patients infected by organisms of Leptospira interrogans serogroup Australis were tested by Western blot to determine the nature of major antigens that are involved in the immune response. Although there was some patient-to-patient variability, immunodominant genus-specific antigens were found to be proteins of apparent molecular ratio 68, 46 and 35-kDa, and lipopolysaccharide (LPS) sub-units in the 35-14-kDa region. Serogroup epitopes specific for Australis were exclusively saccharides of about 32 and 24 kDa: a serovar-specific antigen for serovar lora was of 38-40 kDa and behaved like a protein. Antibodies to the LPS serogroup-specific antigens and to the 38-40 kDa protein were long-lasting and consequently suggest that these Correspondence to:

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Section: Introductionmentioning

confidence: 56%

“…Two or three serum samples were sequentially obtained from six patients who became infected through drinking contaminated water [15]. They have been indicated with the arabic numbers 1, 7,8,9,12,17. Samples were collected: (a) immediately; (b) 18 months; and (c) 36 months after the epidemic outbreak.…”

Section: Human Seramentioning

confidence: 99%

Immunodominant antigens recognized by the human immune response to infection by organisms of the species Leptospira interrogans serogroup Australis

Cinco¹

1992

FEMS Microbiology Letters

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“…Whether this is due to the conformation of the polysaccharide antigen in which its secondary structure may be involved in the binding to antibody is unclear. Antigenic glycolipids in Leptospira interrogans serovar canicola [36,37] and serovar lai [38] have been reported, but their carbohydrate epitope structures have not been determined.…”

Section: Discussionmentioning

confidence: 99%

Immunochemical studies of opsonic epitopes of the lipopolysaccharide of Leptospira interrogans serovar hardjo

Vinh¹

1994

FEMS Immunology and Medical Microbiology

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Leptospiral lipopolysaccharides (LPS) are the main antigens responsible for immunity in leptospirosis. In this investigation we studied the nature of the antigenic determinants of LPS extracted from Leptospira interrogans serovar hardjo (reference strain Hardjoprajitno). The reactions of anti-LPS monoclonal antibodies (mAbs) MUM/F1-4/hardjo (IgM) and MUM/F1-6/hardjo (IgG) with whole cell lysates in Western immunoblotting analysis were unaffected by proteinase K treatment. Periodate treatment of the LPS destroyed the binding of MUM/F1-6/hardjo but preserved that of MUM/F1-4/hardjo. Alkaline phosphatase decreased significantly the binding of MUM/F1-4/hardjo to the LPS but only slightly that of MUM/F1-6/hardjo. On the other hand, phosphodiesterase totally destroyed the binding capacity of both monoclonal antibodies in enzyme immunoassays (EIA). A number of mono- and oligosaccharides was used in EIA inhibition studies. Mannose-6-phosphate and galactose-6-phosphate inhibited the binding of MUM/F1-4/hardjo (50% inhibition at a concentration of 5 mM) to the antigen, but glucose-6-phosphate did not. Galactosamine and mannosamine inhibited the binding of MUM/F1-6/hardjo (50% inhibition at a concentration of 3-4 mM), whereas only a weak inhibition was observed with glucosamine. In contrast, N-acetylated amino sugars did not show any inhibition. An O-acetyl group also appears to be involved in the antigen-antibody binding process.

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“…The variation of affinity constants is considered to be due to difference in the structure of the antigenic determinants. A serovar specific determinant has a carbohydrate nature (16,17), but its structure is still unknown in any serovar . If two serovars have common moieties at a non-reducing end of the carbohydrate sequence but not completely the same sequence, they are cross-reactive and have different affinity constants.…”

Section: Discussionmentioning

confidence: 99%

Affinity Constants of Anti‐Leptospira Monoclonal Antibodies, Numbers of Antigenic Determinants on Leptospiras, and Their Influence on the Microscopic Agglutination Test and ELISA

Takimoto

Ono

Ito

et al. 1988

Microbiology and Immunology

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The affinity constants of anti-canicola and anti-hebdomadis monoclonal antibodies and the numbers of antigenic determinants per organism of each serovar of leptospira were determined, and their influence on the results of microscopic agglutination test (MAT) and ELISA were examined. In the combinations of a monoclonal antibody and some serovar which showed higher affinity constants at levels of 107 to 108/m order, both MAT and ELISA were positive except for one combination, while in the combinations which gave lower affinity constants at levels of 106/m order, MAT was positive but ELISA was negative. The number of antigenic determinants seemed to have no significant influence on the results. The disagreement due to the difference in the threshold affinities of MAT and ELISA should be considered in the use of monoclonal antibodies in the taxonomy of leptospira.Many monoclonal antibodies against various serovars of leptospira interrogans have been produced since the first production described by Ono et al (15). Some were genus-specific (18) or species-specific (3), and others were serogroup-specific (2) or rather serovar-specific (15). Specificities of all monoclonal antibodies have been tested by MAT and/or ELISA. Terpstra et al (20) attempted to use monoclonal antibodies for leptospiral classification by MAT. However, differences in results obtained by MAT and ELISA were found in some monoclonal antibodies; MAT was positive but ELISA was negative, or vice versa (9, 11, 15). These differences cause confusion in the taxonomy of leptospiras by monoclonal antibodies.The present paper deals with the determination of the binding affinities of anti-canicola and anti-hebdomadis monoclonal antibodies for various serovars and the number of antigenic determinants per leptospiral organism in order to explain the difference in the results obtained by MAT and ELISA.

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Isolation of an Antigenic Oligosaccharide Fraction from Leptospira interrogans serovar canicola with a Monoclonal Antibody

Cited by 15 publications

References 15 publications

Immunodominant antigens recognized by the human immune response to infection by organisms of the species Leptospira interrogans serogroup Australis

Immunodominant antigens recognized by the human immune response to infection by organisms of the species Leptospira interrogans serogroup Australis

Immunochemical studies of opsonic epitopes of the lipopolysaccharide of Leptospira interrogans serovar hardjo

Affinity Constants of Anti‐Leptospira Monoclonal Antibodies, Numbers of Antigenic Determinants on Leptospiras, and Their Influence on the Microscopic Agglutination Test and ELISA

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