Leishmania tropica: Characterization of a lipophosphoglycan-like antigen recognized by species-specific monoclonal antibodies

1990 ◽  
Vol 70 (1) ◽  
pp. 12-24 ◽  
Author(s):  
Charles L. Jaffe ◽  
M.Leonor Pérez ◽  
Rive Sarfstein
Keyword(s):  
Monoclonal Antibodies ◽  
Leishmania Tropica ◽  
Species Specific

Generation and Characterization of Species-Specific Anti-Bcl-XL Monoclonal Antibodies

2003 ◽  
Vol 22 (2) ◽  
pp. 91-95 ◽  
Author(s):  
Yi-Te Hsu ◽  
Qi Hou ◽  
Eugene Cymbalyuk ◽  
Richard Youle
Keyword(s):  
Monoclonal Antibodies ◽  
Species Specific

scholarly journals Production and characterization of monoclonal antibodies against Campylobacter fetus subsp. venerealis

2012 ◽  
Vol 32 (7) ◽  
pp. 640-644
Author(s):  
Telma M. Alves ◽  
Luiz G.D. Heneine ◽  
Bárbara S. Araújo ◽  
Luciana M. Silva ◽  
Patrícia C. Campos ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Indirect Elisa ◽  
Spleen Cells ◽  
Myeloma Cells ◽  
Campylobacter Fetus ◽  
Fetus Subsp ◽  
Species Specific ◽  
Limiting Dilution ◽  
Selection Of

Myeloma cells Sp2/0-Ag14 and spleen cells from BALB/c mouse immunized with sonicated Campylobacter fetus subsp. venerealis NCTC 10354 were fused with polyethylene glycol (PEG) for the selection of clones producing antibodies. Clones were obtained by limiting dilution and screened for the production of specific antibodies to C. fetus subsp. venerealis NCTC 10354 by indirect ELISA and western blot against a panel of bacteria: C. fetus subsp. venerealis NCTC 10354, C. fetus subsp fetus ADRI 1812, C. sputorum biovar sputorum LMG 6647, C. lari NCTC 11352, and Arcobacter skirrowii LMG 6621 for the ELISA and C. fetus subsp. venerealis NCTC 10354 and C. sputorum biovar sputorum LMG 6647 for the western blotting. Fifteen clones producing monoclonal antibodies (MAbs) anti-C. fetus subsp. venerealis of the IgM (1) and IgG (14) classes were further screened for species-specificity. Four clones of the 15 obtained were producers of species-specific monoclonal antibodies (MAbs): two were specific for C. fetus subsp. venerealis and two were specific for C. fetus subsp. fetus. None of the clones were reactive against C. sputorum biovar sputorum LMG 6647. All clones recognized a protein with molecular mass of approximately 148 kDa from lysed C. fetus subsp. venerealis NCTC 10354.

Monoclonal antibodies to Leishmania tropica major: specificities and antigen location

Parasitology ◽  
1982 ◽  
Vol 85 (3) ◽  
pp. 523-531 ◽  
Author(s):  
A. A. L. de Ibarra ◽  
J. G. Howard ◽  
D. Snary
Keyword(s):  
Monoclonal Antibodies ◽  
Trypanosoma Cruzi ◽  
Trypanosoma Brucei ◽  
The Other ◽  
Antigenic Determinants ◽  
Leishmania Tropica ◽  
Cell Surfaces ◽  
Species Specific ◽  
Murine Monoclonal Antibodies ◽  
Cellular Organelles

Six murine monoclonal antibodies to Leishmania tropica major have been prepared and the properties of these antibodies studied. Two (WIC 79.3 and 79.7) were L. tropica major species-specific and bound to promastigote cell surfaces, to parasitized macrophages, but not isolated amastigotes. No evidence was found for the production of antibody to the antigenic determinants recognized by WIC 79.3 or 79.7 during L. tropica major infections in mice and hamsters. One antibody (WIC 79.1) bound to sub-cellular organelles of Leishmania species but to a different sub-cellular organelle of Trypanosoma cruzi. Two others bound to the flagellum, one (WIC 79.2) to all Leishmania species, T. cruzi and Trypanosoma brucei, the other (WIC 79.4) only of L. tropica major and L. donovani species. One antibody (WIC 79.5) was directed against an unknown internal antigen found in all Leishmania species and T. cruzi

Characterization of Leishmania isolated in Iran: 1. Serotyping with species specific monoclonal antibodies

Acta Tropica ◽  
2000 ◽  
Vol 75 (3) ◽  
pp. 301-307 ◽  
Author(s):  
S Ardehali ◽  
A Moattari ◽  
G.R Hatam ◽  
S.M.H Hosseini ◽  
I Sharifi
Keyword(s):  
Monoclonal Antibodies ◽  
Species Specific

Characterization of the allergen Der f 7 from house dust mite extracts by species-specific and crossreactive monoclonal antibodies

1997 ◽  
Vol 27 (7) ◽  
pp. 824-832 ◽  
Author(s):  
H.-D. SHEN ◽  
W.-L. LIN ◽  
L.-C. TSAI ◽  
M. F. TAM ◽  
K.-Y. CHUA ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
House Dust ◽  
House Dust Mite ◽  
Dust Mite ◽  
Species Specific

Characterization of Monoclonal Anti-human Factor VII Antibody (B101/B1) that Recognized Three-dimensional Structures near Arg at Position 79 in the First EGF-like Domain

1998 ◽  
Vol 79 (01) ◽  
pp. 104-109 ◽  
Author(s):  
Osamu Takamiya
Keyword(s):  
Monoclonal Antibodies ◽  
Tissue Factor ◽  
Human Factor ◽  
Solid Phase ◽  
Three Dimensional ◽  
Coagulation Factors ◽  
Factor Vii ◽  
Dimensional Structure ◽  
Epidermal Growth

SummaryMurine monoclonal antibodies (designated hVII-B101/B1, hVIIDC2/D4 and hVII-DC6/3D8) directed against human factor VII (FVII) were prepared and characterized, with more extensive characterization of hVII-B101/B1 that did not bind reduced FVIIa. The immunoglobulin of the three monoclonal antibodies consisted of IgG1. These antibodies did not inhibit procoagulant activities of other vitamin K-dependent coagulation factors except FVII and did not cross-react with proteins in the immunoblotting test. hVII-DC2/D4 recognized the light chain after reduction of FVIIa with 2-mercaptoethanol, and hVIIDC6/3D8 the heavy chain. hVII-B101/B1 bound FVII without Ca2+, and possessed stronger affinity for FVII in the presence of Ca2+. The Kd for hVII-B101/B1 to FVII was 1.75 x 10–10 M in the presence of 5 mM CaCl2. The antibody inhibited the binding of FVII to tissue factor in the presence of Ca2+. hVII-B101/B1 also inhibited the activation of FX by the complex of FVIIa and tissue factor in the presence of Ca2+. Furthermore, immunoblotting revealed that hVII-B101/B1 reacted with non-reduced γ-carboxyglutaminic acid (Gla)-domainless-FVII and/or FVIIa. hVII-B101/B1 showed a similar pattern to that of non-reduced proteolytic fragments of FVII by trypsin with hVII-DC2/D4 on immunoblotting test. hVII-B101/B1 reacted differently with the FVII from the dysfunctional FVII variant, FVII Shinjo, which has a substitution of Gln for Arg at residue 79 in the first epidermal growth factor (1st EGF)-like domain (Takamiya O, et al. Haemosta 25, 89-97,1995) compared with normal FVII, when used as a solid phase-antibody for ELISA by the sandwich method. hVII-B101/B1 did not react with a series of short peptide sequences near position 79 in the first EGF-like domain on the solid-phase support for epitope scanning. These results suggested that the specific epitope of the antibody, hVII-B101/B1, was located in the three-dimensional structure near position 79 in the first EGF-like domain of human FVII.

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