Evidence map›Paper›PMID 41651419›Full record

ArticleThe Journal of biological chemistry2026

Development of an inhibitory monoclonal nanobody targeting Streptococcus pyogenes siderophore binding protein FtsB.

Jorge Fernandez-Perez, Susana de Vega, Jose M M Caaveiro, Makoto Nakakido, Satoru Nagatoishi, Akinobu Senoo, Keitaro Tanoi, Takashi Nozawa, Ichiro Nakagawa, Kouhei Tsumoto

Abstract read
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In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

10 authors.

Jorge Fernandez-PerezDepartment of Bioengineering, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Susana de VegaInstitute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Jose M M CaaveiroLaboratory of Protein Drug Discovery, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka, Japan.
Makoto NakakidoDepartment of Bioengineering, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan; Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Satoru NagatoishiDepartment of Bioengineering, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan; Medical Device Development and Regulation Research Center, School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.
Akinobu SenooDepartment of Bioengineering, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan; Laboratory of Protein Drug Discovery, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka, Japan.
Keitaro TanoiGraduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Takashi NozawaDepartment of Microbiology, Graduate School of Medicine, Kyoto University, Sakyo-ku, Kyoto, Japan.
Ichiro NakagawaDepartment of Microbiology, Graduate School of Medicine, Kyoto University, Sakyo-ku, Kyoto, Japan.
Kouhei TsumotoDepartment of Bioengineering, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan; Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan; Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo, Japan; Medical Device Development and Regulation Research Center, School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan. Electronic address: tsumoto@bioeng.t.u-tokyo.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Due to the limited availability of metals inside the human body, pathogenic bacteria must produce multiple highly specialized metal transporters to cause infection. These transporters constitute attractive targets for developing novel antibacterial strategies. Streptococcus pyogenes possesses three iron transporters, of which the FtsABCD system is specialized in the uptake of ferric hydroxamates. The role of this transporter in infection remains unclear. In this study, we developed a monoclonal alpaca VHH, or nanobody, Nb1, targeting FtsB. Nb1 binds to FtsB with sub-nM affinity, in an enthalpy-driven manner, and with a characteristically slow dissociation rate. Solvent accessibility analysis by hydrogen/deuterium exchange coupled with mass spectrometry, mutational analyses, and X-ray crystallography revealed that the epitope of Nb1 is in the binding pocket of FtsB. The nanobody competitively inhibited the binding of multiple hydroxamate siderophores and partially inhibited the uptake of siderophores in S. pyogenes cells. The inhibitory activity of Nb1 on siderophore transport represents a new tool to study the role of the FtsABCD transporter and can be used as a potential inhibitor of S. pyogenes growth under iron-limited conditions.

Indexed as

Antibodies, MonoclonalBacterial ProteinsCarrier ProteinsSiderophoresSingle-Domain AntibodiesStreptococcus pyogenesCrystallography, X-RayAntibodies, MonoclonalBacterial ProteinsCarrier ProteinsSiderophoresSingle-Domain AntibodiesABC transporterepitope mappingFtsBsiderophoresingle-domain antibodyStreptococcus pyogenesuptake inhibitionX-ray crystallography

Identifiers

PMID41651419
PMCPMC12969429

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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.