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Christopher Lynch

Postdoctoral Researcher

I am an early-career postdoc, being awarded a PhD from the Centre for Haematology, Department of Medicine, Imperial College in June 2017. My thesis was focused on using recombinant proteins to understand the mechanisms that regulate the haemostatic functions of the plasma protein von Willebrand Factor and resulted in a number of publications.

I am currently working in Prof. Bhattacharya’s lab in RDM Division of Cardiovascular Medicine, University of Oxford. The focus has been on the recombinant production of chemokine-inhibiting proteins from ticks, firstly to determine underlying mechanisms of chemokine inhibition and second, also to support pre-clinical research projects. 

I have been awarded ‘Young Investigator Awards’ for conference abstracts submitted to the International Society of Thrombosis and Haemostasis (2015) and the European Cell Migration and Chemokine conference (2019).


Publications:

 

1. Lee AW*, Deruaz M*, Lynch C*, Davies G*, Singh K, Alenazi Y, Eaton JRO, Kawamura A, Shaw J, Proudfoot AEI, Dias JM, Bhattacharya S. A knottin scaffold directs the CXC-chemokine-binding specificity of tick evasins. J Biol Chem. 2019 Jul 19;294(29):11199-11212. doi: 10.1074/jbc.RA119.008817. Epub 2019 Jun 5. PMID: 31167786; PMCID: PMC6643034.

(*joint first authors)

This publication identified 27 novel CXCL-inhibiting evasins, including the crystal structure of class founding EVA3 which reveals the protein adopts a knottin-type fold. I contributed to the production and BLI analysis of the 27 proteins and designed the engineered “S5 hybrid” variant to identify a minimal binding region.

 

2. Lynch CJ, Cawte AD, Millar CM, Rueda D, Lane DA. A common mechanism by which type 2A von Willebrand disease mutations enhance ADAMTS13 proteolysis revealed with a von Willebrand factor A2 domain FRET construct. PLoS One. 2017 Nov 29;12(11):e0188405. doi: 10.1371/journal.pone.0188405. PMID: 29186156; PMCID: PMC5706690.

This publication uses a novel FRET construct to monitor the unfolding of the VWFA2 domain. This construct is used to propose a mechanism for point mutations identified from clinical data on patients diagnosed with von Willebrand disease.

 

3. Rye CS, Chessum NE, Lamont S, Pike KG…et al….Lynch CJ, Sharp SY.... et al…..Foote KM, Green S, Workman P, Jones K. Discovery of 4,6-disubstituted pyrimidines as potent inhibitors of the heat shock factor 1 (HSF1) stress pathway and CDK9. Medchemcomm. 2016 Aug 1;7(8):1580-1586. doi: 10.1039/c6md00159a. Epub 2016 Jun 13. PMID: 27746890; PMCID: PMC5048338.

My authorship on this publication arose from my time as a Scientific Offer at the ICR (2009-11). I was author 18/25 and carried out IC50 determination of some of the small molecule compounds. I appreciated having my contribution to the publication recognised, even though I had left five years previously.

4. Lynch CJ, Lane DA. N-linked glycan stabilization of the VWF A2 domain. Blood. 2016 Mar 31;127(13):1711-8. doi: 10.1182/blood-2015-09-672014. Epub 2016 Jan 14. PMID: 26773038; PMCID: PMC4817312.

This publication provides a mechanism for the role of N-linked glycosylation in maintaining protein stability and provides a strategy to test what part of glycan mediates stability and how to replace the need for glycan stabilisation

 

5. Lynch CJ, Lane DA, Luken BM. Control of VWF A2 domain stability and ADAMTS13 access to the scissile bond of full-length VWF. Blood. 2014 Apr 17;123(16):2585-92. doi: 10.1182/blood-2013-11-538173. Epub 2014 Feb 20. PMID: 24558203; PMCID: PMC3990914.

This publication identified the synergy between distinct elements of the VWFA2 domain in controlling unfolding. New protein constructs were developed that allowed complete ADAMTS13 proteolysis of VWF in the absence of denaturant or shear force.