Cell-penetrating peptides (CPPs) are short protein segments that can transport cargos into cells. Although CPPs are widely studied as potential drug delivery tools, their role in normal cell physiology is poorly understood. Early during infection, the L2 capsid protein of human papillomaviruses binds retromer, a cytoplasmic trafficking factor required for delivery of the incoming non-enveloped virus into the retrograde transport pathway. Here, we show that the C terminus of HPV L2 proteins contains a conserved cationic CPP that drives passage of a segment of the L2 protein through the endosomal membrane into the cytoplasm, where it binds retromer, thereby sorting the virus into the retrograde pathway for transport to the trans-Golgi network. These experiments define the cell-autonomous biological role of a CPP in its natural context and reveal how a luminal viral protein engages an essential cytoplasmic entry factor.

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As expected, all tested ligands were capable of forming hydrogen interactions with residues at their respective binding sites, but the DHVA ligand was capable of creating slightly more hydrogen bonds when docked to either 4COX or 5KIR than the other tested ligands, thus demonstrating the participation of this compound in the anti-inflammatory and antialgic responses observed in the in vivo assays as a COX-2 inhibitor. Therefore, the results obtained support the traditional use of OPe for inflammatory and gastric problems.

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Probiotic dairy beverages for lactose intolerants had lactobacilli viability above 7 log CFU for 21 days. The co-cultures studied showed proteolytic activity and reinforced the effect of the jambolan pulp on the antioxidant capacity of the products.

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Correction for ‘Influence of co-cultures of Streptococcus thermophilus and probiotic lactobacilli on quality and antioxidant capacity parameters of lactose-free fermented dairy beverages containing Syzygium cumini (L.) Skeels pulp’ by Sabrina Laís Alves Garcia et al., RSC Adv., 2020, 10, 10297–10308. DOI: 10.1039/c9ra08311a

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