Potentiation of antigen-specific antibody production by peptides derived from Ag85B of Mycobacterium tuberculosis

Kato, Macky; Hanyu, Yoshiro

doi:10.1016/j.jim.2014.12.005

Cited by 1 publication

(3 citation statements)

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“…We showed previously that Peptide-25 derived from Ag85B of M. tuberculosis activated T cells by modulating the Th1/Th2 balance during immunization and thus increased the number of antigen-specific antibody-producing cells [13]. This potentiation was remarkably high in BALB/c mice.…”

Section: Discussionmentioning

confidence: 92%

“…The percentage of antigen-positive IgG and IgM clones was 2.1% and 5.2%, respectively. Without Peptide-1, the percentage of antigen-positive IgG and IgM clones was 0.93% and 3.56%, respectively [13]. Antigen-specific IgG antibody-producing cells increased over two-fold when Peptide-1 was added during IVI.…”

Section: Resultsmentioning

confidence: 99%

“…Thus, Peptide-25 exhibits potent adjuvant activity in both the humoral- and cell-mediated immune responses that appear to be mediated by Th1 cells [12]. We reported previously that antigen-specific antibody production was potentiated by Peptide-25, thus strongly stimulating the production of antigen-specific IgG1 [13]. This potentiation was remarkably high in BALB/c mice (I-A d mice).…”

Section: Introductionmentioning

confidence: 99%

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Potentiating Antigen-Specific Antibody Production with Peptides Obtained from In Silico Screening for High-Affinity against MHC-II

Hanyu

Komeiji

Kato³

2019

Molecules

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Monoclonal antibodies with high affinity and specificity are essential for research and clinical purposes, yet remain difficult to produce. Agretope peptides that can potentiate antigen-specific antibody production have been reported recently. Here, we screened in silico for peptides with higher affinity against the agretope binding pocket in the MHC-II. The screening was based on the 3D crystal structure of a complex between MHC-II and a 14-mer peptide consisting of ovalbumin residues 323–339. Using this 14-mer peptide as template, we constructed a library of candidate peptides and screened for those that bound tightly to MHC-II. Peptide sequences that exhibited a higher binding affinity than the original ovalbumin peptide were identified. The peptide with the highest binding affinity was synthesized and its ability to boost antigen-specific antibody production in vivo and in vitro was assessed. In both cases, antigen-specific IgG antibody production was potentiated. Monoclonal antibodies were established by in vitro immunization using this peptide as immunostimulant, confirming the usefulness of such screened peptides for monoclonal antibody production.

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Section: Discussionmentioning

confidence: 92%

Section: Resultsmentioning

confidence: 99%