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Article Abstract

The family is one of the most economically significant groups of plant RNA viruses, causing severe yield losses in agriculturally important crops. Among the viral proteins encoded by potyviruses, the 6-kilodalton peptide 1 (6K1) has emerged as a critical, albeit poorly understood player in viral pathogenesis. Despite its small size, 6K1 exhibits diverse functions, including facilitating the assembly of viral replication complex (VRC), altering host membrane permeability as a viroporin, and interacting with host factors to promote infection. This review synthesizes current knowledge on 6K1, focusing on its structural characteristics, evolutionary conservation, molecular interactions, and potential as a target for antiviral strategies. We further discuss unresolved questions surrounding its putative ion channel activity, polyprotein processing dynamics, and functional parallels with animal virus viroporins. Understanding 6K1's multifunctionality provides new insights into viral infection mechanisms and opens avenues for novel disease control approaches.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC12176749PMC
http://dx.doi.org/10.3389/fmicb.2025.1605199DOI Listing

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The family is one of the most economically significant groups of plant RNA viruses, causing severe yield losses in agriculturally important crops. Among the viral proteins encoded by potyviruses, the 6-kilodalton peptide 1 (6K1) has emerged as a critical, albeit poorly understood player in viral pathogenesis. Despite its small size, 6K1 exhibits diverse functions, including facilitating the assembly of viral replication complex (VRC), altering host membrane permeability as a viroporin, and interacting with host factors to promote infection.

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Potyviridae, the largest family of plant RNA viruses, includes many important pathogens that significantly reduce the yields of many crops worldwide. In this study, we report that the 6-kilodalton peptide 1 (6K1), one of the least characterized potyviral proteins, is an endoplasmic reticulum-localized protein. AI-assisted structure modeling and biochemical assays suggest that 6K1 forms pentamers with a central hydrophobic tunnel, can increase the cell membrane permeability of and , and can conduct potassium in .

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