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Structural basis of Acinetobacter type IV pili targeting by an RNA virus.
Meng, Ran; Xing, Zhongliang; Chang, Jeng-Yih; Yu, Zihao; Thongchol, Jirapat; Xiao, Wen; Wang, Yuhang; Chamakura, Karthik; Zeng, Zhiqi; Wang, Fengbin; Young, Ry; Zeng, Lanying; Zhang, Junjie.
Afiliación
  • Meng R; Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.
  • Xing Z; Yale University, New Haven, CT, 06520, USA.
  • Chang JY; Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.
  • Yu Z; Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.
  • Thongchol J; UMass Chan Medical School, Worcester, MA, 01655, USA.
  • Xiao W; Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.
  • Wang Y; Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.
  • Chamakura K; Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.
  • Zeng Z; Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.
  • Wang F; Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.
  • Young R; Armata Pharmaceuticals, Inc., Marina del Rey, CA, 90292, USA.
  • Zeng L; Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.
  • Zhang J; Department of Biochemistry and Molecular Genetics, Heersink School of Medicine, University of Alabama at Birmingham, Birmingham, AL, 35294, USA.
Nat Commun ; 15(1): 2746, 2024 Mar 29.
Article en En | MEDLINE | ID: mdl-38553443
ABSTRACT
Acinetobacters pose a significant threat to human health, especially those with weakened immune systems. Type IV pili of acinetobacters play crucial roles in virulence and antibiotic resistance. Single-stranded RNA bacteriophages target the bacterial retractile pili, including type IV. Our study delves into the interaction between Acinetobacter phage AP205 and type IV pili. Using cryo-electron microscopy, we solve structures of the AP205 virion with an asymmetric dimer of maturation proteins, the native Acinetobacter type IV pili bearing a distinct post-translational pilin cleavage, and the pili-bound AP205 showing its maturation proteins adapted to pilin modifications, allowing each phage to bind to one or two pili. Leveraging these results, we develop a 20-kilodalton AP205-derived protein scaffold targeting type IV pili in situ, with potential for research and diagnostics.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Virus ARN / Bacteriófagos / Acinetobacter Límite: Humans Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Virus ARN / Bacteriófagos / Acinetobacter Límite: Humans Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido