Pawar, T. | bioRxiv Science

bioRxiv2026

Spotted fever Rickettsia and relapsing fever Borrelia in rodents from southern India

Bacterial zoonoses constitute a substantial fraction of emerging infectious diseases. In this study, we investigated the presence of pathogenic bacterial genera--Rickettsia, Borrelia, Orientia, Leptospira, and Coxiella--in rodents from southern India. We detected low circulation of Rickettsia (7.26%), Borrelia (6.45%), and Leptospira (0.8%), whereas Orientia and Coxiella were not detected in the rodents sampled. Notably, we observed contrasting patterns of tissue association, with rickettsiae detected exclusively in pooled organ tissues and borreliae detected only in blood, suggesting the influence of pathogen biology in detection probabilities. Our phylogenetic analyses further revealed spotted fever group rickettsiae and relapsing fever group borreliae in both synanthropic and forest-associated rats, highlighting a potential transmission risk to people and livestock in the region. By revealing the circulation of zoonotic bacteria in new host species, this study underscores the need for systematic surveillance of wildlife to better characterize bacterial diversity and its public health implications.

ecology↗

bioRxiv2025

A proteome-wide, MS-based screen identifies SUMOylation of host RNA splicing factors induced by HIV-1 infection

HIV-1 exploits host cell post-translation modifications (PTMs) to facilitate production of infectious particles. These modifications include SUMOylation, a dynamically regulated PTM involving covalent attachment of small ubiquitin-like modifiers (SUMOs) to lysine (K) residues of target proteins. SUMOylation modulates the activity of thousands of proteins and multiple fundamental host cellular processes, including pathways hijacked by HIV-1 to promote infection and spread. The SUMOylation of several proteins during HIV-1 infection has been characterized. However, the broad effects of HIV-1 infection on the SUMOylation of the host cell proteome is largely unknown. To date, SUMOylation has not been explored by large-scale proteomics in the context of HIV infection, where many SUMO-regulated host dependency factors remain to be identified. In this study, we performed a proteome-wide, mass spectrometry (MS)-based screen to identify proteins that are SUMOylated during HIV-1 infection. Here, and in biochemical assays, infection with HIV-1 led to the widespread increased SUMOylation of the heterogeneous nuclear ribonucleoprotein (HNRNP) A/B proteins, a protein family central to the regulation of alternative splicing. Intriguingly, this phenotype was found to be driven by expression of the HIV-1 Viral Infectivity Factor (Vif), suggesting a novel function for this protein aside from APOBEC3G degradation. We selected HNRNPA2B1 (A2/B1) and HNRNPA3 for further study, where depletion of these proteins led to the altered splicing of HIV-1 viral RNAs and dramatically reduced HIV-1 infectivity. Considering the enrichment of SUMOylation sites within the RNA-binding domains of the HNRNPA/B family, our data suggest a novel mechanism involving HIV-1-induced, Vif-mediated SUMOylation of host RNA splicing factors as a means to regulate HIV-1 alternative splicing. Broadly, our findings suggest that infection with HIV-1 alters the SUMOylation of many unexplored host cellular proteins, and provides a significant proteomic resource for their future mechanistic study.

molecular biology↗