Not exact matches
One approach to tackle this challenge is to program into the therapeutic antibodies the capability of
binding to receptors that can help the
MAbs to cross into the brain.
The researchers found that with very few CDR mutations, or even none at all, VH1 - 46
mAbs could
bind with the Dsg3 protein.
(A and B) Pandemic H1N1 reactive
mAbs isolated from infected patients (1000, EM, 70, 1009) were assayed for
binding to annual H1N1 influenza strain whole virus.
This
mAb recognizes a discontinuous epitope on gp 120 and its
binding depends on the tertiary protein structure and intact carbohydrates (1).
This protein
binds to human T - cell receptor CD4 in ELISA and Western ELISA as determined by CD4 / gp120 / Anti gp120
mAb - peroxidase capture ELISA.
mAb 246 - D
binds to overlapping hexapeptides which identified its core epitope as qqLLGIwg (aa 591 - 598) which is located in the immunodominant region (cluster I) of gp41, just upstream from
c) As b) but
bind sCD4 and confirmation dependant
Mabs.
Do not
bind sCD4 or IIIB
mabs recognising conformation dependant epitopes.
Four of the
mAbs, 2T5C9, 2G9C, T1F11, and TB2H7, demonstrated diagnostic potential in enzyme - linked immunosorbent assays (ELISA) by their low to sub-nanomolar cross-reactivity with recombinant wild - type (WT) and mutant TTR aggregates and lack of
binding to native TTR or amyloid fibrils formed by other peptides or proteins.
However,
mAbs had lower maximum
binding signals, indicating that pAbs were required to saturate a diverse collection of
binding sites.
An unconventional (non-CDR) component to pAb's activity was indicated from control human
mAbs, generated against non-amyloid targets,
binding to aggregated Aβ and TTR.
Methods: A novel human
mAb, IRAB - A, was identified by phage screening using competition
binding and surface plasmon resonance assays with the IR extracellular domain.
The Fab fragment of
mAb 5.91, pre-incubated with canine IgE, reduced the
binding of canine IgE to the monocyte cell population from 15 % to 5.6 %.
Moreover, the intact
mAb 5.91 was able to
bind the free IgE to prevent it from
binding cell surface receptors.
This demonstrated that the Fab fragment of
mAb 5.91 was even more effective in reducing the
binding of IgE to the monocyte cell population than the intact
mAb 5.91.
Results showed that the whole
mAb 5.91 molecule reduced the amount of
binding of canine IgE to the monocyte cell population from 15 % to 7.7 %.