Biomedical subjects

Ming Luo

Publications and source records attributed to Ming Luo.

3 recordsLinked to original sources

PubMed2026

Pathogen Species-Specific Differences in Induction of the Maize Polyubiquitin Gene Promoter in Transgenic Wheat.

The maize polyubiquitin promoter (ZmUbi) is a mainstay in molecular biology for transgene expression and is used for constitutive expression of defense-related gene products. Transgenic wheat lines were produced expressing a ZmUbi-RUBY reporter gene that produces the red pigment betalain. Some lines showed transgene silencing with reduced RUBY transcript accumulation and chimeric sectors of betalain. Infection of these plants with Blumeria graminis, Puccinia graminis f. sp. tritici (Pgt), or P. triticina (Pt) each resulted in localized betalain accumulation at infection sites and increased RUBY transcript accumulation. In contrast, two isolates of P. striiformis f. sp. tritici (Pst) caused no detectable RUBY transcript accumulation and no visible betalain accumulation at infection sites, although a modest betalain increase was detected in infected tissue extracts. Compared with Pst, Pgt more strongly induced host genes involved in transcriptional and post-transcriptional regulatory processes, although no obvious pathogen-induced changes in ZmUbi promoter methylation were observed. ZmUbi-GUS transgenic wheat plants were also pathogen challenged, and, unlike Pst, both Pgt and Pt induced localized GUS staining at infection sites. Database mining showed that the endogenous maize polyubiquitin gene from which ZmUbi is derived was pathogen inducible, albeit in a species-specific fashion. These pathogen differences in ZmUbi induction have implications when using this regulatory element to express defense-related transgenes in wheat. Comparing the resistance efficacy of transgenes against different pathogens using this promoter is potentially influenced by significant, localized expression differences occurring at infection sites of different pathogen species. [Formula: see text] Copyright © 2026 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license.

Promoter Regions, Genetic↗

PubMed2026

Comparative in vitro antimicrobial susceptibility profiles of clofazimine and pyrifazimine against clinical isolates of Mycobacterium tuberculosis in southwest China.

UNLABELLED: Clofazimine (CFZ) is a key drug used to treat drug-resistant tuberculosis (DR-TB), while pyrifazimine (TBI-166) is an improved riminophenazine derivative with better pharmacokinetics. However, there is a lack of data on its susceptibility and resistance in regions with a high disease burden, such as southwestern China. We compared the in vitro antimicrobial activities of CFZ and TBI-166 against 249 DR-TB clinical isolates (99 multidrug-resistant TB [MDR-TB] and 150 pre-extensively drug-resistant TB [pre-XDR-TB] isolates) from southwestern China. TBI-166 exhibited a concentration-dependent biphasic antimicrobial pattern compared to CFZ. TBI-166 showed significantly greater potency at low concentrations (MIC₅₀ = 0.031 µg/mL TBI-166 vs 0.25 µg/mL for CFZ; P < 0.001), but attenuated inhibition at high concentrations (MIC₉₀ > 4 µg/mL vs 1 µg/mL for CFZ; P < 0.001). However, at high concentrations, the antibacterial effect of TBI-166 is weaker than that of CFZ (40% of TBI-166-resistant isolates have MIC > 4 µg/mL, compared to 6.67% of CFZ-resistant isolates, P < 0.001). Epidemiological cutoff values (ECOFFs) were 1.0 µg/mL for CFZ and 0.25 µg/mL for TBI-166. Based on these in vitro ECOFFs, the resistance rate to TBI-166 (20.1%, 50/249) was significantly higher than that to CFZ (6.0%, 15/249, P < 0.0001). Whole-genome sequencing revealed that mutations in Rv0678 were prevalent in dual-resistant isolates (10/14) and TBI-166 monoresistant isolates (5/40), while Rv1979c mutations were less frequent, and no pepQ mutations were detected. These mutations differed from known hotspots, suggesting potential novel resistance mechanisms. IMPORTANCE: Drug-resistant tuberculosis (DR-TB) remains a major global health challenge, and optimizing treatments for high-burden regions like southwest China is crucial. This study is the first to detail the differential in vitro activities of clofazimine (CFZ) and the novel TBI-166 against clinical DR-TB isolates from southwest China, alongside their resistance-associated genetic profiles. Findings show TBI-166 has enhanced low-concentration potency but higher resistance rates, plus novel mutations in Rv0678 and Rv1979c linked to resistance. These insights will help refine clinical regimens for DR-TB and strengthen regional resistance surveillance, both of which are essential for controlling the spread of DR-TB in southwest China and informing treatment and surveillance strategies in other similar high-burden areas globally.

Clofazimine↗

PubMed2022

Atomic model of vesicular stomatitis virus and mechanism of assembly.

Like other negative-strand RNA viruses (NSVs) such as influenza and rabies, vesicular stomatitis virus (VSV) has a three-layered organization: a layer of matrix protein (M) resides between the glycoprotein (G)-studded membrane envelope and the nucleocapsid, which is composed of the nucleocapsid protein (N) and the encapsidated genomic RNA. Lack of in situ atomic structures of these viral components has limited mechanistic understanding of assembling the bullet-shaped virion. Here, by cryoEM and sub-particle reconstruction, we have determined the in situ structures of M and N inside VSV at 3.47 Å resolution. In the virion, N and M sites have a stoichiometry of 1:2. The in situ structures of both N and M differ from their crystal structures in their N-terminal segments and oligomerization loops. N-RNA, N-N, and N-M-M interactions govern the formation of the capsid. A double layer of M contributes to packaging of the helical nucleocapsid: the inner M (IM) joins neighboring turns of the N helix, while the outer M (OM) contacts G and the membrane envelope. The pseudo-crystalline organization of G is further mapped by cryoET. The mechanism of VSV assembly is delineated by the network interactions of these viral components.

Animals↗