Ask about this productRelated genes to: TMPRSS11D Blocking Peptide
- Gene:
- TMPRSS11D NIH gene
- Name:
- transmembrane serine protease 11D
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 4q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-03-11
- Date modifiied:
- 2018-01-19
Related products to: TMPRSS11D Blocking Peptide
Related articles to: TMPRSS11D Blocking Peptide
- Proteases are important for the pathogenesis of many viruses. These proteolytic enzymes cleave one or more amide bonds of viral proteins. This protein processing is required for viral entry and replication. The most widely utilized for this purpose are serine proteases, the majority of which are host cell transmembrane, or membrane associated serine proteases such as matriptase, TMPRSS2, TMPRSS11D, and TMPRSS13. Several host cysteine proteases like members of the Cathepsin family (e.g. Cathepsin L) are also highjacked by viruses to process viral proteins to infect their hosts. To target these proteases as antiviral drugs, many inhibitors, both competitive and covalent, have been developed but none have been advanced to clinical evaluation to date. Herein, we review these proteases, their viral protein substrates, pathogenesis, and their inhibitors. - Source: PubMed
Banas VictoriaMannino Michael PJanetka James W - Neuroinflammation plays a central role in neurodegenerative diseases such as Alzheimer's and Parkinson's, along with depression, anxiety, and infectious diseases including COVID-19. Harmine and harmaline, β-carboline alkaloids from , exhibit immunomodulatory, anti-inflammatory, and neuroprotective properties. In this study, we aimed not only to investigate the anti-inflammatory and neuroprotective effects of β-carbolines and extract on a lipopolysaccharide (LPS)-induced neuroinflammation model using SH-SY5Y cells and their impact on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) receptor expression but also to compare cytokine levels in plasma from intensive care unit (ICU) and non-ICU COVID-19 patients, thereby providing clinical context for the inflammatory response. - Source: PubMed
Publication date: 2026/01/26
Bianco Laura SeixasNicoliche TiagoCorrêa-Neto Nelson FranciscoLanaro RafaelCaetano Ariadiny LPrado Carla MaximoUreshino Rodrigo PortesTibério Iolanda de Fátima Lopes CalvoRighetti Renato FragaStilhano Roberta SessaLinardi Alessandra - Coronaviruses not only hijack host cells to serve as viral factories but also exploit host proteolytic systems to activate their spike (S) protein, the key glycoprotein mediating receptor binding and membrane fusion. Feline coronavirus (FCoV), which initially replicates in the intestinal tract, has evolved to utilize local intestinal proteases for S protein activation. This activation occurs through proteolytic cleavage at specific regions on the S protein, known as cleavage sites (CSs). Two putative CSs have been proposed for FCoV: S1/S2 CS and S2' CS. Through a protease screen, we identified serine proteases as particularly critical for FCoV infection. Notably, three pancreatic serine proteases, chymotrypsin, trypsin, and elastase, enhanced FCoV infection and promoted syncytia formation despite their differing cleavage specificities, suggesting a flexible activation strategy. Furthermore, the membrane-bound serine proteases TMPRSS2 and TMPRSS11D also facilitated infection and syncytia formation in a strain-dependent manner. By analyzing the cleavage profiles of these serine proteases, we experimentally confirmed these two putative CSs on the FCoV S protein and identified additional CSs. Importantly, our analysis revealed a compensatory cleavage mechanism at the S2' CS that maintains spike activation even when mutations disrupt the canonical cleavage motif, underscoring the central role of S2' CS in viral infection. Additionally, an acidic microenvironment is required for efficient infection. Together, these findings illustrate how FCoV adapts to locally available serine proteases to optimize S protein priming and intestinal cell entry. - Source: PubMed
Publication date: 2026/01/08
Chen BixiaVanden Buijs LunaVanderheijden NathalieDesmarets LowieseVan Cleemput JolienNauwynck Hans J - TMPRSS2 and HAT (or TMPRSS11D) are host serine proteases critically involved in the entry of several respiratory viruses, including SARS-CoV-2. To our knowledge, no dual inhibitors targeting both enzymes have been reported to date. Here, we describe a series of -aminobenzylamine derivatives acting as potent dual TMPRSS2/HAT non-covalent inhibitors. In SARS-CoV-2 infection assays in lung epithelial cells, four compounds demonstrated significant antiviral activity without cytotoxicity at tested doses. Drug-likeness profiling confirmed compliance with Lipinski's and Veber's rules, as well as favourable solubility and microsomal stability. These findings highlight a novel chemical series with potential as broad-spectrum antivirals targeting host proteases. - Source: PubMed
Publication date: 2025/10/28
Carvaillo HélèneDussol AshokChaaya NancyKadri SaraSoualmia FeryelMasurier NicolasEl Amri Chahrazade - Transmembrane Protease, Serine-2 (TMPRSS2) and TMPRSS11D are human proteases that enable SARS-CoV-2 and Influenza A/B virus infections, but their biochemical mechanisms for facilitating viral cell entry remain unclear. We show these proteases spontaneously and efficiently cleave their own zymogen activation motifs, activating their broader protease activity on cellular substrates. We determine TMPRSS11D co-crystal structures with a native and an engineered activation motif, revealing insights into its autocleavage activation and distinct substrate binding cleft features. Leveraging this structural data, we develop nanomolar potency peptidomimetic inhibitors of TMPRSS11D and TMPRSS2. We show that a broad serine protease inhibitor that underwent clinical trials for TMPRSS2-targeted COVID-19 therapy, nafamostat mesylate, was rapidly cleaved by TMPRSS11D and converted to low activity derivatives. In this work, we develop mechanistic insights into human protease viral tropism and highlight both the strengths and limitations of existing human serine protease inhibitors, informing future drug discovery efforts targeting these proteases. - Source: PubMed
Publication date: 2025/05/10
Fraser Bryan JWilson Ryan PFerková SáraIlyassov OlzhasLac JackieDong AipingLi Yen-YenSeitova AlmaLi YanjunHejazi ZahraKenney Tristan M GPenn Linda ZEdwards AledLeduc RichardBoudreault Pierre-LucMorin Gregg BBénard FrançoisArrowsmith Cheryl H