Antigen-antibody recognition and mechanics at single molecule scale

L. Limozin, , P. Robert, PH. Puech

Collaboration:  P. Chames (CRCM), F. Piazza (Univ. Orléans)

The laminar flow chamber was used on an antibody-antigen model, demonstrating a possible complex energy landscape characterized by a rough part (Biophys. J. 2011) and influenced by molecular environment at nanometer scale (Int. J. Nanotech. 2013). Adding systematic temperature variation to the method allowed us to measure this roughness (Sci. reports, 2016). A major point to understand receptor clustering is to quantify multiple bond breaking. We compared single to double antigen–antibody binding to dissect avidity mechanisms (PLoS ONE 2012). Through further improvements in the method, we measured the effect of much larger forces, both as ramps or steady force, necessary for multiple bond maturation and breaking studies (in preparation).


Survival curves at different applied forces for two anti-CD16 nanobodies. Left: survival decreases with force (slip bond). Right: survival increases with force (catch bond)

Aside, we investigate kinetic binding properties of single domain antibodies and have found the first antibody, to our knowledge, which exhibit catch-bond like behavior (Gonzalez 2019).

Gonzalez C, Chames P, Kerfelec B, Baty D, Robert P, Limozin L (2019). Biophys. J. 116: 1516-1526. Pubmed.

Limozin L, Bongrand P , Robert P (2016) Sci. Rep. 6:35193. Pubmed

Lo Schiavo V, P. Robert, L. Limozin, P. Bongrand (2012) PLoS ONE 7:e44070. Pubmed

Robert P , Nicolas A, Aranda-Espinoza S, Bongrand P, Limozin L (2011) Biophys. J. 100 : 2642-2651. Pubmed