Plasmodium falciparum: Production and Characterization of Rat Monoclonal Antibodies Specific for the Sexual-Stage Pfs48/45 Antigen

2001 ◽  
Vol 97 (1) ◽  
pp. 45-49 ◽  
Author(s):  
W Roeffen ◽  
K Teelen ◽  
J van As ◽  
M vd Vegte-Bolmer ◽  
W Eling ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Monoclonal Antibodies ◽  
Sexual Stage

Characterization of two in vivo challenge models to measure functional activity of monoclonal antibodies to Plasmodium falciparum circumsporozoite protein

2020 ◽  
Author(s):  
Rama Raghunandan ◽  
Bryan T Mayer ◽  
Yevel Flores-Garcia ◽  
Monica W Gerber ◽  
Raphael Gottardo ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Monoclonal Antibodies ◽  
Functional Activity ◽  
Statistical Power ◽  
Rank Order ◽  
Circumsporozoite Protein ◽  
Dose Selection ◽  
Selection Of

Abstract Background New strategies are needed to reduce the incidence of malaria, and promising approaches include the development of vaccines and monoclonal antibodies (mAbs) that target the circumsporozoite protein (CSP). To select the best candidates and speed development, it is essential to standardize preclinical assays to measure the potency of such interventions in animal models. Methods Two assay configurations were studied using transgenic Plasmodium berghei expressing Plasmodium falciparum full-length circumsporozoite protein. The assays measured 1) reduction in parasite infection of the liver (liver burden) following an intravenous (i.v) administration of sporozoites and 2) protection from parasitaemia following mosquito bite challenge. Two human CSP mAbs, AB311 and AB317, were compared for their ability to inhibit infection. Multiple independent experiments were conducted to define assay variability and resultant impact on the ability to discriminate differences in mAb functional activity. Results Overall, the assays produced highly consistent results in that all individual experiments showed greater functional activity for AB317 compared to AB311 as calculated by the dose required for 50% inhibition (ID50) as well as the serum concentration required for 50% inhibition (IC50). The data were then used to model experimental designs with adequate statistical power to rigorously screen, compare, and rank order novel anti-CSP mAbs. Conclusion The results indicate that in vivo assays described here can provide reliable information for comparing the functional activity of mAbs. The results also provide guidance regarding selection of the appropriate experimental design, dose selection, and group sizes.

Characterization of Plasmodium falciparum sexual stage antigens and their biosynthesis in synchronised gametocyte cultures

1986 ◽  
Vol 20 (2) ◽  
pp. 155-163 ◽  
Author(s):  
Arno N. Vermeulen ◽  
Jan van Deursen ◽  
Ruud H. Brakenhoff ◽  
Ton H.W. Lensen ◽  
Thivi Ponnudurai ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Sexual Stage

scholarly journals Characterization of two in vivo challenge models to measure functional activity of monoclonal antibodies to Plasmodium falciparum circumsporozoite protein

2020 ◽  
Vol 19 (1) ◽  
Author(s):  
Rama Raghunandan ◽  
Bryan T. Mayer ◽  
Yevel Flores-Garcia ◽  
Monica W. Gerber ◽  
Raphael Gottardo ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Monoclonal Antibodies ◽  
Functional Activity ◽  
Circumsporozoite Protein

scholarly journals Production and characterization of specific monoclonal antibodies binding the Plasmodium falciparum diagnostic biomarker, histidine-rich protein 2

2014 ◽  
Vol 13 (1) ◽  
Author(s):  
Chiuan Herng Leow ◽  
Martina Jones ◽  
Qin Cheng ◽  
Stephen Mahler ◽  
James McCarthy
Keyword(s):  
Plasmodium Falciparum ◽  
Monoclonal Antibodies ◽  
Diagnostic Biomarker

scholarly journals Recombinant Pfs25 protein of Plasmodium falciparum elicits malaria transmission-blocking immunity in experimental animals.

1991 ◽  
Vol 174 (5) ◽  
pp. 1203-1208 ◽  
Author(s):  
P J Barr ◽  
K M Green ◽  
H L Gibson ◽  
I C Bathurst ◽  
I A Quakyi ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Monoclonal Antibodies ◽  
Recombinant Dna ◽  
Vaccine Candidate ◽  
Mosquito Vector ◽  
Sexual Stage ◽  
Transmission Blocking ◽  
Experimental Animals ◽  
Potential Vaccine ◽  
Blocking Antibodies

Pfs25 is a sexual stage antigen of Plasmodium falciparum that is expressed on the surface of zygote and ookinete forms of the parasite. Monoclonal antibodies directed against native Pfs25 can block completely the development of P. falciparum oocysts in the midgut of the mosquito vector. Thus, this 25-kD protein is a potential vaccine candidate for eliciting transmission-blocking immunity in inhabitants of malaria endemic regions. We have synthesized, by secretion from yeast, a polypeptide analogue of Pfs25 that reacts with conformation-dependent monoclonal antibodies, and elicits transmission-blocking antibodies when used to immunize mice and monkeys in conjunction with a muramyl tripeptide adjuvant. Our results suggest the further evaluation of recombinant DNA-derived Pfs25 in transmission-blocking vaccination studies in humans.

The characterization of two monoclonal antibodies which react with high molecular weight antigens of asexual Plasmodium falciparum

1992 ◽  
Vol 54 (2) ◽  
pp. 231-246 ◽  
Author(s):  
S HANDUNNETTI ◽  
B PASLOSKE ◽  
M VANSCHRAVENDIJK ◽  
J AGUIAR ◽  
T TARASCHI ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Plasmodium Falciparum ◽  
Monoclonal Antibodies ◽  
High Molecular Weight

scholarly journals Isolation, production and characterization of fully human monoclonal antibodies directed to Plasmodium falciparum MSP10

2015 ◽  
Vol 14 (1) ◽  
Author(s):  
Dominika J Maskus ◽  
Susanne Bethke ◽  
Melanie Seidel ◽  
Stephanie Kapelski ◽  
Otchere Addai-Mensah ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Monoclonal Antibodies ◽  
Human Monoclonal Antibodies

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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