HNRNPM promotes protein synthesis via an interaction with stem-loop 5 in the SARS-CoV-2 5'-UTR
- 1Archives School Marburg
Abstract
The 5'-untranslated region (5'-UTR) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is highly structured and comprises five conserved stem-loops that serve as cis-acting regulatory elements. During infection, host proteins are recruited to these elements and regulate multiple steps during the viral life cycle. Stem-loop 5 (SL5) is highly conserved among different alpha- and betacoronaviruses and includes the start codon of non-structural protein 1 (nsp1). However, the function of SL5 in viral replication and its interacting proteins remain to be determined. Here, we identified heterogeneous nuclear ribonucleoprotein M (HNRNPM) as a host protein functionally interacting with SL5. HNRNPM translocates into the cytoplasm during SARS-CoV-2 infection and promotes protein synthesis from the viral 5'-UTR. Mutations in the lower stem of SL5 impair HNRNPM binding and reduce protein synthesis. Notably, the interaction between HNRNPM and SL5 is conserved among different alpha- and betacoronaviruses. Our findings indicate that HNRNPM is an important host factor that regulates viral translation to promote SARS-CoV-2 replication.
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BibTeX
@misc{golagha2026hnrnpm,
title = {{HNRNPM promotes protein synthesis via an interaction with stem-loop 5 in the SARS-CoV-2 5'-UTR}},
author = {J. Golagha and M. Wieja and N. Biedenkopf and J. E. Weigand},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.05.756635},
url = {https://www.biorxiv.org/content/10.64898/2026.10.05.756635v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - HNRNPM promotes protein synthesis via an interaction with stem-loop 5 in the SARS-CoV-2 5'-UTR
AU - J. Golagha
AU - M. Wieja
AU - N. Biedenkopf
AU - J. E. Weigand
PY - 2026
DA - 2026/10/05
PB - bioRxiv
DO - 10.64898/2026.10.05.756635
UR - https://www.biorxiv.org/content/10.64898/2026.10.05.756635v1
AB - The 5'-untranslated region (5'-UTR) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is highly structured and comprises five conserved stem-loops that serve as cis-acting regulatory elements. During infection, host proteins are recruited to these elements and regulate multiple steps during the viral life cycle. Stem-loop 5 (SL5) is highly conserved among different alpha- and betacoronaviruses and includes the start codon of non-structural protein 1 (nsp1). However, the function of SL5 in viral replication and its interacting proteins remain to be determined. Here, we identified heterogeneous nuclear ribonucleoprotein M (HNRNPM) as a host protein functionally interacting with SL5. HNRNPM translocates into the cytoplasm during SARS-CoV-2 infection and promotes protein synthesis from the viral 5'-UTR. Mutations in the lower stem of SL5 impair HNRNPM binding and reduce protein synthesis. Notably, the interaction between HNRNPM and SL5 is conserved among different alpha- and betacoronaviruses. Our findings indicate that HNRNPM is an important host factor that regulates viral translation to promote SARS-CoV-2 replication.
ER -