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Paucarmayta, A.

Publications and source records attributed to Paucarmayta, A..

2 recordsLinked to original sources

Mechanisms regulating combination effect of antibody-drug conjugates and cancer immunotherapy

Antibody-drug conjugates (ADCs) have emerged as a transformative class of cancer therapeutics with important challenges still to be addressed. Combination of ADC with immunotherapy is a promising strategy but mechanisms and effective application remain to be determined. We evaluated ADC combinations with T cell engagers (TCEs) and checkpoint inhibitors (CPI). ADC-TCE combinations produced robust antitumor activity independent of antigen and payload and persisted despite ADC-related T cell loss. Efficacy was dominated by a direct effect of ADC on tumor cells. ADCs induced autophagy that upregulated TNF receptors (TNFRs) and mannose-6-phosphate receptors (M6PR). When ADCs were combined with TCEs TNF released by T cells was primarily responsible for potent antitumor effect of combination. In contrast, M6PR was dispensable for ADC-TCE activity but critical for combinations with CPI expanded antigen-specific T cells via enhanced granzyme B uptake. These data reveal a unifying, target- and payload-agnostic mechanism enabling rational ADC-immunotherapy combinations. SignificanceThis is first evidence that ADC-induced tumor cell autophagy via up-regulation of TNFR and M6PR could be responsible for potent antitumor effect of combination of ADC with TCE. TCEs exploit a TNF-TNFR axis, whereas antigen-specific T cells leverage granzyme B-M6PR uptake. This mechanistic framework explains broad ADC-TCE synergy and guides rational selection of ADC-immunotherapy combinations beyond checkpoint blockade.

immunology↗

Cancer immunotherapy by NC410, a LAIR-2 Fc protein blocking LAIR-collagen interaction

Collagens are a primary component of the extracellular matrix and are functional ligands for the inhibitory immune receptor leukocyte associated immunoglobulin-like receptor-1 (LAIR-1). Leukocyte associated immunoglobulin-like receptor-2 (LAIR-2) is a secreted protein that can act as a decoy receptor by binding collagen with higher affinity than LAIR-1. We propose that collagens promote immune evasion by interacting with LAIR-1 and that LAIR-2 could release LAIR-1 mediated immune suppression. Analysis of public datasets shows high LAIR-2 expression being associated with a favorable outcome in certain tumors. We designed a dimeric LAIR-2 with a functional IgG1 Fc tail, NC410, and showed that NC410 reduces tumor growth and increases T cell expansion and effector function in humanized tumor models. Immunohistochemical analysis of human tumors shows that NC410 binds to collagen-rich areas where LAIR-1+ immune cells are localized. Our findings show that NC410 might be a powerful new strategy for cancer immunotherapy for immune-excluded tumors.

cancer biology↗