Evidence map›Paper›PMID 41309228›Full record

ArticleJournal of microbiology (Seoul, Korea)2025

Encapsulin protein MAV2054 enhances Mycobacterium avium virulence by promoting Cdc42-dependent epithelial cell invasion.

Dong Ho Kim, I Jeong Jo, Min Ju Kang, Yi Seol Kim, Duyen Do Tran Huong, Kyungho Woo, Ho-Sung Park, Hwa-Jung Kim, Chul Hee Choi

Abstract read
In one paragraph

Article in Journal of microbiology (Seoul, Korea), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Dong Ho KimDepartment of Microbiology, School of Medicine, Chungnam National University, Daejeon 35015, Republic of Korea.
I Jeong JoDepartment of Microbiology, School of Medicine, Chungnam National University, Daejeon 35015, Republic of Korea.
Min Ju KangDepartment of Microbiology, School of Medicine, Chungnam National University, Daejeon 35015, Republic of Korea.
Yi Seol KimDepartment of Microbiology, School of Medicine, Chungnam National University, Daejeon 35015, Republic of Korea.
Duyen Do Tran HuongDepartment of Microbiology, School of Medicine, Chungnam National University, Daejeon 35015, Republic of Korea.
Kyungho WooDepartment of Microbiology, School of Medicine, Chungnam National University, Daejeon 35015, Republic of Korea.
Ho-Sung ParkDepartment of Microbiology, School of Medicine, Chungnam National University, Daejeon 35015, Republic of Korea.
Hwa-Jung KimDepartment of Microbiology, School of Medicine, Chungnam National University, Daejeon 35015, Republic of Korea.
Chul Hee ChoiDepartment of Microbiology, School of Medicine, Chungnam National University, Daejeon 35015, Republic of Korea.

Funding

Korea Health Industry Development InstituteMinistry of Education RS-2023-00273828Ministry of Health and Welfare RS-2022-KH130308Ministry of Health and Welfare RS-2024-00336984Ministry of Science and ICT RS-2024-00406568National Research Foundation of Korea
6 · The paper itself

Abstract

Mycobacterium avium complex (MAC) organisms are widespread environmental pathogens associated with chronic pulmonary infections. Although M. avium is known to invade epithelial cells, the molecular mechanisms underlying this process remain incompletely understood. In this study, we identified a novel role for MAVRS09815 (formerly MAV2054), a family 2A encapsulin nanocompartment shell protein, in mediating bacterial adhesion, epithelial cell invasion, and in vivo virulence. We engineered a recombinant M. smegmatis strain expressing MAV2054 (Ms_2054) and an M. avium MAV2054 deletion mutant (Δ2054). Ms_2054 exhibited enhanced epithelial invasion, whereas Δ2054 showed reduced intracellular survival. Recombinant MAV2054 protein was bound directly to human epithelial cells in a dose-dependent manner. Pretreatment of host cells with cytochalasin D or vinblastine significantly inhibited bacterial internalization, indicating that MAV2054-mediated invasion is cytoskeleton-dependent. Confocal and scanning electron microscopy revealed MAV2054-dependent membrane rearrangements during infection. Pull-down assays demonstrated that MAV2054 activates Cdc42, a key regulator of actin polymerization, with reduced activation observed in Δ2054-infected cells. In a murine intratracheal infection model, the Δ2054 exhibited significantly reduced bacterial burdens and lung inflammation compared to the wild type. These findings demonstrate that MAV2054 enhances M. avium virulence by promoting epithelial cell invasion through Cdc42-dependent cytoskeletal remodeling. This study reveals a previously unrecognized role for an encapsulin-like protein in host-pathogen interactions and highlights its potential as a therapeutic target in MAC infections.

Indexed as

cdc42 GTP-Binding ProteinEpithelial CellsHost-Pathogen InteractionsMycobacterium aviumActinsAnimalsBacterial AdhesionCell LineCytochalasin DCytoskeletonFemaleHumansMiceMice, Inbred C57BLVinblastineVirulenceActinscdc42 GTP-Binding ProteinCytochalasin DVinblastineactin cytoskeleton remodelingencapsulin nanocompartmentMAV2054Mycobacterium avium

Identifiers

PMID41309228
PMCPMC13577054

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.