Crystallographic Structure of Porcine Adenovirus Type 4 Fiber Head and Galectin Domains

Author:

Guardado-Calvo Pablo1,Muñoz Eva M.2,Llamas-Saiz Antonio L.3,Fox Gavin C.4,Kahn Richard4,Curiel David T.5,Glasgow Joel N.56,van Raaij Mark J.17

Affiliation:

1. Departamento de Bioquímica y Biología Molecular, Facultad de Farmacia

2. Departamento de Química Orgánica, Facultad de Química

3. Unidad de Rayos X, Laboratorio Integral de Dinámica y Estructura de Biomoléculas José R. Carracido, Universidad de Santiago de Compostela, E-15782 Santiago de Compostela, Spain

4. Laboratoire de Proteines Membranaires, Institut de Biologie Structurale J.P. Ebel, F-38027 Grenoble, France

5. Division of Human Gene Therapy, Departments of Medicine, Obstetrics and Gynecology, Pathology, Surgery, the Gene Therapy Center

6. Division of Cardiology, University of Alabama at Birmingham, Birmingham, Alabama

7. Departamento de Biología Estructural, Instituto de Biología Molecular de Barcelona (CSIC), E-02808 Barcelona, Spain

Abstract

ABSTRACT Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locating both sugar binding sites face to face. Sequence evidence suggests other tandem-repeat galectins have the same arrangement. We show that the galectin domain binds carbohydrates containing lactose and N -acetyl-lactosamine units, and we present structures of the galectin domain with lactose, N -acetyl-lactosamine, 3-aminopropyl-lacto- N -neotetraose, and 2-aminoethyl-tri( N -acetyl-lactosamine), confirming the domain as a bona fide galectin domain.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Cited by 20 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. From examining the relationship between (corona)viral adhesins and galectins to glyco-perspectives;Biophysical Journal;2021-03

2. Virus recognition of glycan receptors;Current Opinion in Virology;2019-02

3. Structure and N-acetylglucosamine binding of the distal domain of mouse adenovirus 2 fibre;Journal of General Virology;2018-11-01

4. Three-Dimensional Structures of Galectins;Trends in Glycoscience and Glycotechnology;2018

5. Three-Dimensional Structures of Galectins;Trends in Glycoscience and Glycotechnology;2018

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