The <i>Helicobacter pylori</i> adhesin protein HopQ exploits the dimer interface of human CEACAMs to facilitate translocation of the oncoprotein CagA.

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作者： Daniel A,Bonsor ^[1] ; Qing,Zhao ^[2] ; Barbara,Schmidinger ^[2] ; Evelyn,Weiss ^[2] ; Jingheng,Wang ^[3] ; Daniel,Deredge ^[4] ; Robert,Beadenkopf ^[1] ; Blaine,Dow ^[1] ; Wolfgang,Fischer ^[2] ; Dorothy,Beckett ^[3] ; Patrick L,Wintrode ^[4] ; Rainer,Haas ^[2] ; Eric J,Sundberg ^[5]

作者单位： Institute of Human Virology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD, USA. ^[1] Chair of Medical Microbiology and Hospital Epidemiology, Max von Pettenkofer Institute, Faculty of Medicine, LMU Munich, Munich, Germany. ^[2] Department of Chemistry and Biochemistry, University of Maryland, College Park, MD, USA. ^[3] Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, USA. ^[4] German Center for Infection Research (DZIF), Partner Site LMU, Munich, Germany. ^[5] Institute of Human Virology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD, USA esundberg@ihv.umaryland.edu. ^[6] Department of Medicine, University of Maryland School of Medicine, University of Maryland, Baltimore, MD, USA. ^[7] Department of Microbiology and Immunology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD, USA. ^[8]

关键词 CEACAM Helicobacter pylori CagA HopQ X‐ray crystallography