Biology subjects

Lim, Y. T.

Publications and source records attributed to Lim, Y. T..

2 recordsLinked to original sources

bioRxiv2025

Host mRNA 3'-end processing machinery are critical binding partners during dengue virus infection

Dengue virus (DENV) causes a wide variety of dengue diseases that threaten over half of the worlds population. At present, there is no antiviral therapeutics against dengue. Virus infection and its associated pathologies are the result of a myriad of interactions between the virus and its host, of which most are protein-protein interactions (PPIs). Virus-encoded proteins modulate the host environment for the virus benefit by interacting with host proteins during infection. Thus studies of these virus-host PPIs are most informative when performed in the context of an infection. We undertook a comparative affinity purification-mass spectrometry approach to generate a DENV-host protein-protein interactome during DENV infection and identified mRNA 3-end processing protein complexes as novel interactors of DENV NS3. We demonstrated that the presence of the cleavage and polyadenylation specificity factor complex proteins, but not their enzymatic activity, is crucial for DENV replication, thus unveiling a potential new direction for the development of host-directed antiviral therapeutics.

microbiology↗

bioRxiv2022

Complete sequences of the velvet worm slime proteins reveal that slime formation is enabled by disulfide bonds and intrinsically disordered regions

The slime of velvet worms (Onychophora) is a strong and fully biodegradable protein material, which upon ejection undergoes a fast liquid-to-solid transition to ensnare prey. However, the molecular mechanisms of slime self-assembly are still not well understood, notably because the primary structures of slime proteins are yet unknown. Combining transcriptomic and proteomic studies, we have obtained the complete primary sequences of slime proteins and identified key features for slime self-assembly. The high molecular weight slime proteins contain Cys residues at the N- and C-termini that mediate the formation of multi-protein complexes via disulfide bonding. Low complexity domains in the N-termini were also identified and their propensity for liquid-liquid phase separation established, which may play a central role for slime biofabrication. Using solid-state nuclear magnetic resonance, rigid and flexible domains of the slime proteins were mapped to specific peptide domains. The complete sequencing of major slime proteins is an important step towards sustainable fabrication of polymers inspired by the velvet worm slime.

bioengineering↗