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Biology subjects

Duncan, M. C.

Publications and source records attributed to Duncan, M. C..

4 recordsLinked to original sources

HIV superinfection reveals sequential reservoir reactivation and immune-driven rebound dynamics

Superinfection, where a person with HIV acquires a second phylogenetically distinct strain, provides an opportunity to study reservoir evolutionary dynamics because the two strains can be tracked over time. We here characterize such a case that originally went undetected by clinical monitoring. The participant, who expressed the protective HLA-B*57:03 allele, initially controlled his subtype B infection but lost control after superinfection with a unique recombinant form (URF), which came to dominate in plasma without displacing the original B strain. Five years after initiating therapy, replication-competent proviruses from both strains persisted in blood, though URF proviruses dominated (80%). Despite their unequal reservoir representation, both strains rapidly rebounded upon treatment interruption, though most rebounding sequences belonged to a URF subclade that predated ART initiation. During the treatment interruption, genetically distinct viral lineages continually appeared in plasma, consistent with sequential "waves" of reactivation of diverse reservoir clones. Notably, immune escape variants emerged from the reservoir in a later "wave", displacing initial susceptible variants and underscoring the important role of immune responses in shaping rebound dynamics. Sequence analysis revealed that the URF transmitted/founder virus already harbored key HLA-B*57:03-associated escape mutations, likely explaining the loss of viral control after superinfection. Our results reveal that superinfection can remain undetected despite routine HIV clinical monitoring, that pre-adaptation of the superinfecting strain to host HLA can undermine immune control, that rebound virus can originate from reservoir clones predating ART initiation, and that immune responses can actively shape rebound dynamics by driving escape variant outgrowth during treatment interruption. IMPORTANCEThis case demonstrates that HIV superinfection can go undetected by routine clinical monitoring, underscoring the importance of assays that capture HIV diversity -- particularly those used to screen participants for cure trials. It also illustrates how pre-adaptation of a superinfecting strain to host HLA-restricted immune responses can evade existing immunity, with implications for understanding natural immune control, and underscoring the challenge of viral diversity for vaccine and immunotherapy design. The sequential emergence of genetically diverse HIV lineages during treatment interruption, including minority immune escape variants that emerged from the reservoir to displace the initial susceptible population, highlights the difficulty of predicting rebound virus composition and underscores the key role of immune responses in shaping rebound dynamics. Critically, escaped rebound variants can then reseed the reservoir, thereby enriching it in escaped forms, highlighting a specific vulnerability for cure approaches that harness natural immune responses to eliminate reservoir cells.

molecular biology↗

The endo-lysosomal system drives lumen formation in a human epiblast model

The formation of a central lumen in the epiblast is a critical step that occurs during implantation in the human embryo. Lumen formation is accompanied by highly dynamic and complex cargo trafficking in the endo-lysosomal system. However, our understanding of key players and machineries that control this critical trafficking process remains incomplete in the context of epiblast development. Here, we explored endo-lysosomal dynamics that are associated with the generation of the apicosome, the earliest stage of lumen formation in a model of human epiblast development based on human pluripotent stem cells. We uncovered a hybrid early/late endosome compartment as well as a previously unrecognized dynamics of late endosome and lysosome compartments in trafficking podocalyxin (PODXL), a sialomucin glycoprotein that helps to establish and maintain the open lumen, during apicosome formation. To gain molecular insight into these unique hybrid endosome and late endosome/lysosome machineries in PODXL traffic, we used APEX2-based spatial proteomics to identify PODXL-proximity partners during apicosome formation, and identified RAB35, a Rab small GTPase known to control PODXL traffic as well as early and late endosome dynamics, as a key player in controlling apicosome formation. Our results suggest that RAB35 limits excess apicosome formation by promoting the early to late endosome transition as well as lysosome formation, which help to reduce PODXL to a level necessary for single apicosome formation. Overall, this study reveals novel endo-lysosomal mechanisms that contribute to apical membrane morphogenesis in a human model of epiblast formation.

developmental biology↗

Characterization of a high-intensity band that cross-reacts with FLAG-M2 antibodies in immunoblots in a subset of laboratory strains of Saccharomyces cerevisiae.

Epitope tags are commonly used for various purposes in research labs. The DYKDDDDK-peptide epitope, trademarked as the FLAG epitope, is a commonly used epitope tag. It is often used for monitoring protein levels and for affinity chromatography. Multiple DYKDDDDK-binding antibodies are available; however, the mouse monoclonal anti-FLAG M2 is widely used due to its commercial availability in several formats. Many laboratory Saccharomyces cerevisiae strains, including the BY4741 strain that was used in multiple systematic deletion and tagging libraries, have a high-intensity band that cross-reacts with the FLAG-M2 antibody. The presence of this high-intensity cross-reactive band can be problematic in some applications. Here, we show that despite high-intensity in immunoblots, the cross-reacting band is not enriched by FLAG-M2 affinity beads under native conditions. We also report the fortuitous identification of a strain closely related to BY4741 that lacks the high-intensity cross-reactive band. Finally, contrary to anecdotal reports, we determined that the high-intensity cross-reacting band is not Rtf1. These findings and resources should assist other researchers using the DYKDDDDK-epitope for immunoblots and affinity chromatography.

cell biology↗

Two functionally distinct HEATR5 protein complexes are defined by fast-evolving co-factors in yeast

The highly conserved HEATR5 proteins are best known for their roles in membrane traffic mediated by the adaptor protein complex-1 (AP1). HEATR5 proteins rely on fast-evolving co-factors to bind to AP1. However, how HEATR5 proteins interact with these co-factors is unknown. Here, we report that the budding yeast HEATR5 protein, Laa1, functions in two biochemically distinct complexes. These complexes are defined by a pair of mutually exclusive Laa1-binding proteins, Laa2 and the previously uncharacterized Lft1/Yml037c. Despite limited sequence similarity, biochemical analysis and structure predictions indicate that Lft1 and Laa2 bind Laa1 via structurally similar mechanisms. Both Laa1 complexes function in intra-Golgi recycling. However, only the Laa2-Laa1 complex binds to AP1 and contributes to its localization. Finally, structure predictions indicate that human HEATR5 proteins bind to a pair of fast-evolving interacting partners via a mechanism similar to that observed in yeast. These results reveal mechanistic insight into how HEATR5 proteins bind their co-factors and indicate that Laa1 performs functions besides recruiting AP1.

cell biology↗