Related Experiment Video
Updated: Jul 4, 2026

Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance
Published on: October 16, 2018
Structural basis of multimodal adsorption and infection initiation by Vibrio phage Peru-2
Huaxin Yu1,2, Justin Zhao1,2,3, Jian Yue1,2
1Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT 06516, USA.
Abstract:
Phage Peru-2, isolated during the 1993 cholera outbreaks in Peru, is distinct from the three ICP phage lineages typically associated with epidemic Vibrio cholerae. The molecular basis of Peru-2 adsorption and infection initiation has remained unknown. Here, we combine single-particle cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET) to define the architecture and infection mechanisms of Peru-2 at high resolution. The mature virion comprises an icosahedral capsid decorated with minor capsid proteins and a short tail apparatus surrounded by six structurally flexible tailspikes. These tailspikes are enzymatically active in mediating phage attachment to the Vibrio polysaccharide (VPS), a key component of biofilms. Three internal core proteins form a disordered core adjacent to the portal, positioning them for release before genome ejection during infection initiation. Structural analyses further resolve pre-ejection, genome-ejection, and post-ejection intermediates of the tail apparatus, while cryo-ET imaging of infected cells reveals a multimodal adsorption strategy during infection initiation.
Insights
Phage Peru-2, a unique Vibrio cholerae virus, uses flexible tailspikes to attach to biofilms via Vibrio polysaccharide. Its distinct structure and multimodal adsorption strategy offer new insights into phage-bacterial interactions.
Area of Science:
- Structural biology
- Microbiology
- Virology
Background:
- Phage Peru-2, isolated during Peruvian cholera outbreaks, differs from typical epidemic Vibrio cholerae phages.
- The molecular mechanisms of Peru-2's adsorption and infection initiation were previously unknown.
- Understanding Vibrio phage adsorption is crucial for their ecological and evolutionary roles.
Purpose of the Study:
- To determine the high-resolution architecture of Phage Peru-2.
- To elucidate the infection mechanisms of Phage Peru-2.
- To understand the host recognition and adsorption strategies of Vibrio phages.
Main Methods:
- Single-particle cryo-electron microscopy (cryo-EM) for high-resolution structure determination.
- Cryo-electron tomography (cryo-ET) for imaging infected cells and infection intermediates.
- Functional assays to assess the role of Vibrio polysaccharide (VPS) in adsorption.
Main Results:
- The mature Peru-2 virion structure was resolved, revealing an icosahedral capsid, minor capsid proteins, and flexible tailspikes.
- Tailspikes were found to be enzymatically active, mediating attachment to Vibrio polysaccharide (VPS).
- Cryo-ET revealed multimodal adsorption strategies, including interaction with bacterial cell surface and flagella, and identified infection intermediates.
Conclusions:
- Phage Peru-2 possesses a unique structure with flexible tailspikes essential for VPS-mediated attachment.
- Peru-2 employs multiple adsorption strategies distinct from T7-like phages.
- The study provides a mechanistic framework for understanding Vibrio phage-host interactions.
Related Concept Videos
Bacteriophages of the Human Virome
Lytic Cycle of Bacteriophages
Regulation of Bacterial Virulence
Viral Replication: Lytic Cycle
DNA Bacteriophages
Intracellular Movement of Viruses and Bacteria

