Anti-MHCII [VHH7]

Description:

Recombinant monoclonal antibody to MHCII. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the alpaca peripheral lymphocyte VHH7.

Clone Name:

VHH7

Published Application(s):

Blocking, in vitro, in vivo, IP, SPR, FC, IF, Imaging

Published Species Reactivity:

Mouse

Alternative Name(s) of Target: class II MHC; class II histocompatibility antigen
Immunogen: The original antibody was generated by immunizing an alpaca with intact, unfractionated mouse splenocytes seven times.

Specificity: This antibody is specific for mouse MHCII.

Application Notes: This nanobody was linked to an anti-GFP VHH via their C termini to create a bispecific antibody capable of targeting both GFP and MHC class II Molecules; the VHH7-GFP bispecific construct effectively targeted B cells and facilitated the uptake of GFP by these cells, as indicated by a flow cytometry (FC) analysis that showed that most CD19⁺ cells were GFP⁺, indicating successful capture of GFP in vivo. The same bispecific antibody was used to stain B cells in mouse lymph node cells, as observed using FC. This nanobody was also used to C-terminally conjugate human IL2 and IFN-α to anti-GFP, demonstrating the general applicability of the approach for linking different entities (Witte et al., 2012; PMID: 22778432). This nanobody was used as a control in a competition assay, where it was compared to a panel of NP-specific VHHs and used to block recombinant NP before immunoprecipitation (IP) (Ashour et al., 2015; PMID: 25540369). As part of its characterization, this nanobody's K_a, K_d, and K_D were evaluated for polymorphic MHCII variants through binding experiments. Also, its binding capacity to recombinant MHCII-CLIP was measured by surface plasmon resonance (SPR). A fluorescently labeled variant of this nanobody was used to track the internalization of VHH-receptor complexes and acidic subcellular compartments. This nanobody was used in vivo to investigate its effects on immune responses and antibody production; it was found to activate CD8^- dendritic cells, leading to stronger CD4 T cell proliferation than other antibodies tested (DC13 and DC20). This nanobody effectively delivered proteins or peptides to antigen-presenting cells, generating humoral immunity; fusion of antigens to this nanobody was found to enhance the immune response compared to other delivery methods — mice immunized with this nanobody fused to antigens such as GFP, yeast ubiquitin, OBI-17mer peptide, or influenza HA stem exhibited potent humoral responses, which were further enhanced by the dimeric version of this nanobody. VHH7-H3N2 HA212-63 immunization improved protection against influenza infection (Duarte et al., 2016; PMID: 27821668).

Antibody first published in: Duarte et al. Generation of Immunity against Pathogens via Single-Domain Antibody-Antigen Constructs J Immunol. 2016 Dec 15;197(12):4838-4847. doi: 10.4049/jimmunol.1600692 PMID:27821668
Note on publication: The original publication describes the development and application of single-domain antibody fragments (VHHs), such as VHH7, as targeted antigen-delivery vehicles for enhancing immune responses in antigen-presenting cells.

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