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Biology subjects

Menon, K.

Publications and source records attributed to Menon, K..

4 recordsLinked to original sources

A post-translational regulatory map of chronic antigen-driven human T cell dysfunction.

T cells exposed to persistent antigen in the context of chronic viral infections or cancer lose self-renewal and cytotoxic capacity. Several transcriptional, epigenetic, and metabolic drivers of this process have been identified. However, the post-transcriptional regulatory mechanisms influencing the proteome of dysfunctional T cells are not well understood. Here we present a time-resolved molecular landscape of human T cells during the development of chronic antigen-driven dysfunction. Persistent T cell receptor stimulation significantly remodeled the proteome, including changes in canonical T cell exhaustion-associated proteins and proteins related to mitochondrial function, redox homeostasis, nucleotide metabolism, and cell-cycle progression. Dysfunctional T cells displayed activation of stress response pathways that were recapitulated in vivo; targeting these pathways altered the cytotoxic capacity of T cells during persistent tumor exposure. Our comprehensive proteomic resource reveals unique post-transcriptional changes in dysfunctional T cells and lays the groundwork for novel cysteine-directed therapeutics to enhance cancer immunotherapy.

immunology↗

AlphaFold3 for Structure-guided Ligand Discovery

Deep-learning methods for protein structure prediction, such as AlphaFold2 (AF2) and RosettaFold (RF), have transformed structural biology and accelerated downstream biological discovery. More recent models, including AlphaFold3 (AF3) and RosettaFold All-Atom (RFAA), extend this capability to protein-ligand co-folding, enabling direct prediction of bound complexes from sequence and ligand inputs. This advance has raised the possibility that such models could function not only as structure predictors but also as AI-based molecular docking engines for virtual screening. Yet their true impact on ligand discovery remains unclear and, in many cases, controversial. Here, we systematically assess AF3 co-folding across tasks central to small-molecule discovery compared to conventional molecular docking. First, retrospective enrichment of actives over decoys showed that AF3 outperforms the physics-based docking program DOCK3 across 43 drug targets in DUDE-Z; however, this advantage is largely driven by hidden ligand-only biases inherent to computational decoy sets. In contrast, in three large experimental datasets (the sigma-2 receptor ({sigma}2), the D4 dopamine receptor (D4), AmpC {beta}-lactamase (AmpC)) with over 2,500 tested molecules that lack such biases, DOCK3 achieved stronger overall enrichment, while AF3 contributed mainly to early enrichment. Second, out-of-sample pose reproduction on >8,000 protein-ligand complexes deposited after the AF3 training and validation cutoff showed that AF3 accuracy is strongly dependent on training-set similarity, indicating that the model memorizes atomic positions more than learning general principles of molecular recognition. Finally, in the first prospective head-to-head screen against the {sigma}2 receptor, novel to AF3s training set, AF3 achieved a 13% hit rate and identified a 13 nM binder directly from the screen. However, compared with the parallel DOCK3 campaign, AF3 delivered a two-fold lower hit rate, despite yielding a similar affinity distribution among the top five hits. A crystal structure of the {sigma}2 receptor bound to the most potent AF3-derived hit confirmed that AF3 produced a near-native ligand pose. AF3 therefore represents the beginning of deep-learning-based structure-guided ligand discovery: a complementary tool rather than a replacement for conventional docking, with practical applications both as a screening engine and as a post-docking filter that improves hit rates. More broadly, this work establishes a framework for evaluating next-generation deep-learning co-folding models and quantifying their impact on small-molecule discovery.

pharmacology and toxicology↗

Outsmarting refractory glioblastoma using in silico guided, phage display derived peptides targeting oncogenic EGFRvIII

EGFRvIII mutation contributes to tumor aggressiveness and poor prognosis in multiple cancers. Despite being tumor-specific, EGFRvIII are not readily detected since they coexist with EGFR. Here, we developed novel, aqueous-dispersible peptides (1-15 kDa) that can detect and actively target EGFRvIII expressing refractory tumors, while sparing wild-type EGFR and normal astrocytes. Based on in silico molecular modeling, docking and biologics-based approaches, four EGFRvIII-targeting peptides were identified using phage display technology employing a) antibody fragments (AF), and b) random peptide library (RPL). Among RPL-based peptides, RB5 showed appreciable interactions with EGFRvIII receptor, as indicated by binding energy of -10.6 kcal/mol, in silico. In vitro binding studies using ELISA and immunocytochemistry further confirmed that RB5 could specifically target EGFRvIII+ glioblastoma cell, U87MG.{Delta}EGFR. Interestingly, AF-based peptide, H13, also showed considerable specificity towards U87MG.{Delta}EGFR. Importantly, these peptides exerted no cytotoxicity (MTS assay), or affected the downstream phosphorylation (western blot) in EGFRvIII cells. Thus, our study demonstrated that rationally designed peptide molecules can precisely target EGFRvIII tumors with minimal or no intracellular signaling interference. Owing to simple molecular architectures, these non-toxic, aqueous-dispersible peptides hold strong potential for conjugation with antitumor drugs and therapeutic nanoparticles for treating EGFRvIII positive refractory cancers.

molecular biology↗

Interactions with presynaptic photoreceptors mediated by the Dpr11 and DIP-γ cell surface proteins control selection and survival of Drosophila amacrine neurons

Drosophila R7 UV photoreceptors (PRs) are divided into yellow (y) and pale (p) subtypes with different wavelength sensitivities. yR7 PRs express the Dpr11 cell surface protein and are presynaptic to Dm8 amacrine neurons (yDm8) that express Dpr11s binding partner DIP-{gamma}, while pR7 PRs synapse onto DIP-{gamma}-negative pDm8 neurons. Dpr11 and DIP-{gamma} expression patterns define yellow and pale medulla color vision circuits that project to higher-order areas. DIP- {gamma} and dpr11 mutations affect the morphology of yDm8 arbors in the yellow circuit. yDm8 neurons are generated in excess during development and compete for presynaptic yR7 partners. Transsynaptic interactions between Dpr11 and DIP-{gamma} are required for generation of neurotrophic signals that allow yDm8 neurons to survive. yDm8 and pDm8 neurons do not normally compete for neurotrophic support, but can be forced to do so by manipulating R7 subtype fates. DIP-{gamma}-Dpr11 interactions allow yDm8 neurons to select yR7 PRs as their home column partners.

neuroscience↗