Bispecific antibodies targeting multiple regions of the SARS-CoV-2 spike protein comparably neutralize variants of concern and wild-type virus.

A functional human IgA response to malaria targets a conserved epitope in the N terminus of the Plasmodium falciparum circumsporozoite protein.

Heterotrimeric G proteins are signal transducers acting downstream of seven transmembrane receptors. However, recent studies in C. elegans and in Drosophila have revealed another essential function of these proteins in positioning and pulling force of the mitotic spindle during asymmetrical cell division. We previously reported the localization of a member of the RGS family, RGS14 in the centrosomes. In this study, we report localization of Gi subfamily of heterotrimeric G protein in the centrosomes and midbody of mammalian cells. Gi1 and Gi2, but not Gi3, localize in the centrosomes of interphase and mitotic cells. During cytokinesis Gi1 is localized in the midbody, but absent from the centrosome, Gi2 is present in both, and Gi3 is in the midbody. Using FRET analysis we show that RGS14‐CFP and Giα1‐YFP interact in the centrosomes. RGS14 possesses two Gi‐interacting domains, an RGS domain and a GoLoco domain. As expected, no positive FRET signal is detected when a RGS14‐CFP deletion mutant that lacks both these domains is co‐expressed in centrosomes with Gi1‐YFP. A point mutant in which both the RGS and GoLoco domains are defective in Gi binding is also unable to generate positive FRET signals. However, mutants containing either the Gi binding‐defective RGS or GoLoco domain show positive FRET signals, suggesting that RGS14 binds Gi1 in the centrosomes via both the RGS and GoLoco domains. Our results demonstrate for the first time the interaction between a Gi and a RGS protein in the centrosomes of mammalian cells, opening a new chapter for studying the role of heterotrimeric G and RGS proteins in centrosome physiology and function.

Leishmaniasis is a vector-borne disease transmitted by female sand flies infected with Leishmania parasites. Cutaneous leishmaniasis is primarily caused by Leishmania major in the Old World and typically manifests as skin ulcers. The carbohydrate-rich molecules on the surface of Leishmania are crucial for the parasite's infectivity in the vertebrate host and vector. Among these, galactose moieties have been identified as promising targets for vaccines against leishmaniasis. This study investigates the potential of human monoclonal antibodies (mAbs) targeting α-Gal to prevent L major infection. Our results demonstrate that α-Gal–specific mAbs effectively bind to and agglutinate metacyclic and procyclic L major promastigotes. To assess the protective efficacy of these mAbs, we challenged α1,3-galactosyltransferase–deficient mice with L major. The mAb AG030 significantly delayed the onset of skin lesions and reduced the parasite burden. These findings provide proof of principle that α-Gal–targeting mAbs could serve as an intervention to prevent cutaneous leishmaniasis.