scholarly journals Immunization with Bovine Serum Albumin (BSA) in Oil-Adjuvant Elicits IgM Antibody Response in Chinese Soft-Shelled Turtle (Pelodiscus Sinensis)

Vaccines ◽  
2020 ◽  
Vol 8 (2) ◽  
pp. 257
Author(s):  
Cheng Xu ◽  
Jiehao Xu ◽  
Yu Chen ◽  
Øystein Evensen ◽  
Hetron Mweemba Munang’andu ◽  
...  

Immunoassays are among the frontline methods used for disease diagnosis and surveillance. Despite this, there are no immunoassays developed for the Chinese soft-shelled turtle (Pelodiscus sinensis), which has expanded into large scale commercial production in several Asian countries. One of the critical factors delaying the development of immunoassays is the lack of characterized soft-shelled turtle immunoglobulins. Herein, we used mass spectrometry together with the ProtQuest software to identify the soft-shelled turtle IgM heavy chain in serum, which again was used to produce a polyclonal anti-turtle-IgM in rabbits. Thereafter, the polyclonal anti-turtle-IgM was used as a secondary antibody in an indirect ELISA to evaluate antibody responses of soft-shelled turtles injected with the bovine serum albumin (BSA) model antigen. Our findings show that only turtle immunized with a water-in-oil BSA plus ISA 763A VG adjuvant (SEPPIC, France) emulsion had antibodies detected at 42 days post vaccination (dpv) while turtles injected with phosphate buffered saline (PBS) only as well as turtle injected with BSA dissolved in PBS had no significant antibody levels detected in serum throughout the study period. In summary, our findings show that rabbit polyclonal anti-turtle-IgM produced can be used in ELISA to measure serum antibody responses in immunized soft-shelled turtles. Future studies should explore its application in other immunoassays needed for the disease diagnosis and vaccine development for soft-shelled turtles.

2020 ◽  
Vol 56 (90) ◽  
pp. 13959-13962
Author(s):  
Han Lin ◽  
Haofei Hong ◽  
Jinfeng Wang ◽  
Chen Li ◽  
Zhifang Zhou ◽  
...  

Rhamnose and sTn antigen were co-conjugated to bovine serum albumin (BSA) for cancer vaccine development. The immune responses against sTn have been significantly augmented with the involvement of Rha-specific antibodies to enhance antigen uptake.


2003 ◽  
Vol 4 (4) ◽  
pp. 157-161 ◽  
Author(s):  
Francisco Perez-Bravo ◽  
Amaya Oyarzun ◽  
Elena Carrasco ◽  
Cecilia Albala ◽  
Janice S. Dorman ◽  
...  

Nanomaterials ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 276 ◽  
Author(s):  
Xiaoqing Yu ◽  
Shuwei Sun ◽  
Lin Zhou ◽  
Zhicong Miao ◽  
Xiaoyuan Zhang ◽  
...  

Here we report the fabrication of graphene oxide (GO)-based membranes covalently combined with bovine serum albumin (BSA) for metal ions detection. In this system, BSA acts as a transporter protein in the membrane and endows the membrane with selective recognition of Co2+, Cu2+, AuCl4−, and Fe2+. Combining the metal-binding ability of BSA and the large surface area of GO, the hybrid membrane can be used as a water purification strategy to selectively absorb a large amount of AuCl4− from HAuCl4 solution. Moreover, BSA could reduce the membrane-immobilized AuCl4− by adding sodium borohydride (NaBH4). Interestingly, adsorption experiments on three kinds of metal ions showed that the GO–BSA membrane had good selective adsorption of Co2+ compared with Cu2+ and Fe2+. The morphology and composition changes of the membrane were observed with atomic force microscopy (AFM) and Raman spectroscopy, respectively. It is expected that this facile strategy for fabricating large-scale graphene-biomolecule membranes will spark inspirations in the development of functional nanomaterials and wastewater purification.


1963 ◽  
Vol 117 (6) ◽  
pp. 1035-1051 ◽  
Author(s):  
Maria C. Michaelides ◽  
Albert H. Coons

Rabbits were injected into the hind foot with diphtheria toxoid and bovine serum albumin. Fragments of popliteal lymph node taken from them several months later were placed in plasma-clot cultures with Eagle's medium. When antigen was added to the culture fluid, anamnestic antibody responses occurred regularly. When the antigen was diphtheria, responsiveness remained for 4 days after the beginning of the culture. When it was bovine serum albumin, responsiveness lasted for about 8 days. Once an anamnestic response had begun, antibody formation continued for 4 weeks or more. High concentrations of bovine serum albumin (0.5 mg/ml) did not inhibit the response. When both antigens were used to stimulate the same culture, it was found that the two responses were independent.


2010 ◽  
Vol 38 (2) ◽  
pp. 215-220 ◽  
Author(s):  
CHRISTOPHER SJÖWALL ◽  
ALF KASTBOM ◽  
GUNNEL ALMROTH ◽  
JONAS WETTERÖ ◽  
THOMAS SKOGH

Objective.To evaluate (1) to what extent sera from healthy subjects and patients with rheumatoid arthritis (RA) contain antibodies to bovine serum albumin (BSA); and (2) if anti-BSA antibodies interfere with results of enzyme-linked immunoassays (ELISA) containing BSA.Methods.The ELISA used was a previously developed in-house assay of autoantibodies to tumor necrosis factor (TNF). Anti-TNF and anti-BSA antibodies were analyzed by ELISA in 189 patients with early RA and 186 healthy blood donors. TNF preparations containing either BSA or human serum albumin (HSA) as carrier proteins were used as antigens in the anti-TNF assay. The presence and levels of antibodies were analyzed in relation to disease course and to the presence/absence of rheumatoid factor (RF).Results.In patients with RA, anti-TNF/BSA levels strongly correlated with anti-BSA levels (r = 0.81, p < 0.001), whereas anti-TNF/HSA did not (r = −0.09). Neither the presence nor the levels of anti-BSA in RA patients were associated with disease progression, and antibody levels were not significantly altered compared to controls (p = 0.11). IgG reactivity with TNF/HSA was neglible. In paired sera, preincubation with BSA abolished the anti-TNF/BSA reactivity. There were no indications of RF interference with anti-BSA or anti-TNF reactivity.Conclusion.Antibodies to BSA are common in patients with RA as well as in healthy individuals. Their presence does not seem to be associated with RA disease activity or disease course, but may severely interfere with ELISA containing BSA. The use of BSA as a “blocking agent” or carrier protein in immunoassays should therefore be avoided.


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