ArticleMolecular biology reports2026
Recombinant maltose-inducible porin LamB of Aeromonas hydrophila induces T
Article in Molecular biology reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
backgroundAeromonas hydrophila is a major freshwater fish pathogen responsible for significant economic losses to the aquaculture industry. Its virulence factors include proteins involved in primary adhesion, pili, flagella, O-antigen, outer membrane proteins, and adhesins, etc. Among these, the outer membrane maltose-inducible porin functions as an adhesin and can be a potential vaccine candidate. METHODS AND
resultsIn the present study, the maltose-inducible porin (LamB) of A. hydrophila was heterologously overexpressed, purified and assessed for its immunogenic potential in a murine model. The gene encoding mature LamB was cloned into pRSET-A expression vector. Recombinant LamB (rLamB) carrying a 6×-histidine tag was expressed as inclusion bodies in E. coli BL21(λDE3), purified from solubilized inclusion bodies by metal affinity chromatography to near homogeneity, and refolded. Immunization of mice with rLamB generated high-titer anti-rLamB antibodies with high specificity. The anti-rLamB antisera agglutinated live A. hydrophila cells in vitro and recognized other Aeromonas species, suggesting its possible application in the diagnosis of Aeromonas infection and potential as a candidate for broad-spectrum vaccine development. Antibody isotyping and cytokine ELISA indicated a T
conclusionRecombinant LamB of Aeromonas hydrophila elicited strong and specific immune responses, generating high-titer antibodies that agglutinated live bacteria and cross-reacted with other Aeromonas species. These findings collectively suggest that rLamB of A. hydrophila may have potential as a vaccine candidate for broad-spectrum vaccine development and possible diagnostic applications against heterogeneous A. hydrophila.
Indexed as
Identifiers
42183925What OpenQuestion holds
Registered trials
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 OpenQuestion graph.