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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	The structural basis for Z α1-antitrypsin polymerization in the liver Sarah V. Faull , Emma L. K. Elliston , Bibek Gooptu , Alistair M. Jagger , Ibrahim Aldobiyan , Adam Redzej , Magd Badaoui , Nina Heyer-Chauhan , S. Tamir Rashid , Gary M. Reynolds , David H. Adams , Elena Miranda , Elena V. Orlova , James A. Irving , David A. Lomas Science Advances 6 DOI: 10.1126/sciadv.abc1370 Diamond Proposal Number(s): [17201] Open Access Show Abstract ▼ Abstract: The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self-association of proteins into ordered aggregates. α1-Antitrypsin deficiency is the archetypal serpinopathy and results from the formation and deposition of mutant forms of α1-antitrypsin as “polymer” chains in liver tissue. No detailed structural analysis has been performed of this material. Moreover, there is little information on the relevance of well-studied artificially induced polymers to these disease-associated molecules. We have isolated polymers from the liver tissue of Z α1-antitrypsin homozygotes (E342K) who have undergone transplantation, labeled them using a Fab fragment, and performed single-particle analysis of negative-stain electron micrographs. The data show structural equivalence between heat-induced and ex vivo polymers and that the intersubunit linkage is best explained by a carboxyl-terminal domain swap between molecules of α1-antitrypsin.	Oct 2020
	Re-evaluation of human BDCA-2+ DC during acute sterile skin inflammation Yi-Ling Chen , Tomas Gomes , Clare S. Hardman , Felipe A. Vieira Braga , Danuta Gutowska-Owsiak , Maryam Salimi , Nicki Gray , David A. Duncan , Gary Reynolds , David Johnson , Mariolina Salio , Vincenzo Cerundolo , Jillian L. Barlow , Andrew N. J. Mckenzie , Sarah A. Teichmann , Muzlifah Haniffa , Graham Ogg The Journal Of Experimental Medicine 217 DOI: 10.1084/jem.20190811 Show Abstract ▼ Abstract: Plasmacytoid dendritic cells (pDCs) produce type I interferon (IFN-I) and are traditionally defined as being BDCA-2+CD123+. pDCs are not readily detectable in healthy human skin, but have been suggested to accumulate in wounds. Here, we describe a CD1a-bearing BDCA-2+CD123int DC subset that rapidly infiltrates human skin wounds and comprises a major DC population. Using single-cell RNA sequencing, we show that these cells are largely activated DCs acquiring features compatible with lymph node homing and antigen presentation, but unexpectedly express both BDCA-2 and CD123, potentially mimicking pDCs. Furthermore, a third BDCA-2–expressing population, Axl+Siglec-6+ DCs (ASDC), was also found to infiltrate human skin during wounding. These data demonstrate early skin infiltration of a previously unrecognized CD123intBDCA-2+CD1a+ DC subset during acute sterile inflammation, and prompt a re-evaluation of previously ascribed pDC involvement in skin disease.	Mar 2020

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