P10930

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Research Report: Enterobacteria phage T4 gene 12 (gp12 short tail fiber protein; UniProt P10930)

0) Identity verification and scope control (critical)

The target described in UniProt (P10930) is gene product 12 (gp12) from Enterobacteria phage T4, annotated as the short tail fiber protein. Across structural and mechanistic literature, “gene 12 / gp12” in T4 consistently refers to the baseplate-anchored short tail fiber (STF) that participates in adsorption to Gram-negative hosts by binding lipopolysaccharide (LPS) core structures and is trimeric. This matches the UniProt-provided family/domain context (tevenvirinae STF; “Short_tail_fibre_C” etc.). (thomassen2003thestructureof pages 1-2, raaij2001crystalstructureof pages 1-2, leiman2010morphogenesisofthe pages 2-5)

Limitation: within the retrieved full text, the UniProt accession P10930 is not explicitly mentioned, so the UniProt↔literature mapping is supported by concordant name/organism/function/domain evidence rather than an explicit accession cross-reference. (thomassen2003thestructureof pages 1-2, leiman2010morphogenesisofthe pages 2-5)

1) Key concepts and definitions (current understanding)

1.1 Short tail fibers (STFs) vs long tail fibers (LTFs)

In T4-like myophages, adsorption is commonly conceptualized as a two-stage process: initial, reversible surface engagement (often dominated by long tail fibers) followed by an irreversible (or pseudo-irreversible) commitment step mediated by short tail fibers. In contemporary terminology, gp12 forms the STF and is the component responsible for pseudo-irreversible binding to a secondary receptor such as LPS. (kleinsousa2024towardsacomplete pages 1-4, mourosi2022understandingbacteriophagetail pages 9-11)

1.2 Receptor-binding proteins (RBPs)

RBPs are the virion components that contact host receptors (outer membrane proteins, glycans/exopolysaccharides, flagella). Tail fibers/spikes are prominent RBPs. Modern work emphasizes modularity of RBPs (N-terminal attachment modules + C-terminal receptor-recognition modules), which underpins host-range evolution and engineering. (kleinsousa2024towardsacomplete pages 1-4)

1.3 “Pseudo-irreversible” binding

The term reflects that adsorption can be extremely stable due to multivalency (multiple binding sites per fiber and multiple fibers per virion), even if individual interactions may be reversible. A structure-based model for gp12 proposes multiple LPS-binding grooves per trimer, and six STF trimers per phage increases avidity, shifting the overall interaction to quasi-irreversible. (thomassen2003thestructureof pages 5-7, leiman2010morphogenesisofthe pages 2-5)

2) Primary function and biological role of gp12

2.1 Role in infection: irreversible anchoring to LPS core

gp12 forms the short tail fibers of bacteriophage T4 and mediates irreversible binding to the host by binding the core region of Escherichia coli LPS. This is explicitly stated in primary structural papers on gp12 receptor-binding domains. (thomassen2003thestructureof pages 1-2, raaij2001crystalstructureof pages 1-2)

A mechanistic model for T4 infection initiation describes how, after long-tail-fiber-mediated receptor searching and transmission of a mechanical signal to the baseplate, short tail fibers are unpinned, rotate downward, and irreversibly bind the lipid A–inner core region of LPS; this anchoring is coupled to baseplate rearrangements that enable tail sheath contraction and genome delivery. (mourosi2022understandingbacteriophagetail pages 9-11)

2.2 Receptor specificity: LPS core (inner-core/lipid A proximal)

Across sources, receptor binding is consistently localized to LPS core structures, with some sources phrasing the bound epitope as “core region of LPS” and others specifying “lipid A–inner core region.” (thomassen2003thestructureof pages 1-2, raaij2001crystalstructureof pages 1-2, mourosi2022understandingbacteriophagetail pages 9-11)

A 2024 preprint summarizing tail-fiber diversity explicitly identifies T4 gp12 STF as responsible for pseudo-irreversible binding to LPS as a secondary receptor. (kleinsousa2024towardsacomplete pages 1-4)

3) Localization and assembly context (where gp12 acts)

3.1 Virion localization

gp12 is part of the T4 tail baseplate apparatus, localized at the baseplate outer rim, with 18 copies per tail (6 STF trimers). (leiman2010morphogenesisofthe pages 2-5)

3.2 Attachment interfaces and assembly partners

Short tail fibers are parallel homotrimers. Structural reviews describe that gp12 N-termini attach to gp10 trimers in the baseplate, while gp11 trimers hold the short tail fibers at a hinge roughly halfway along the fiber—placing gp12 within a defined baseplate attachment/hinge architecture. (hyman2018bacteriophaget4long pages 6-7)

4) Molecular features: structure, domains, and determinants of function

4.1 Oligomeric state and size

Multiple sources describe gp12 as a parallel, in-register homotrimer with 527 residues per subunit. (hyman2018bacteriophaget4long pages 6-7, thomassen2003thestructureof pages 1-2, raaij2001crystalstructureof pages 1-2)

Leiman et al. summarize gp12 as ~55.3 kDa per monomer, trimeric, with 18 copies per tail. (leiman2010morphogenesisofthe pages 2-5)

4.2 Structural architecture relevant to receptor binding

Primary X-ray crystallography of gp12 fragments established that the short tail fiber contains a right-handed triple-stranded β-helix and a C-terminal globular receptor-binding region. (raaij2001crystalstructureof pages 1-2, thomassen2003thestructureof pages 5-7)

A high-resolution receptor-binding domain structure (reported at 1.5 Å) reveals a knitted trimeric fold with a head/bonnet subdivision and proposes that the positively charged apex and grooves lined with aromatic/basic residues form the LPS-binding surface(s). (thomassen2003thestructureof pages 1-2, thomassen2003thestructureof pages 5-7)

Earlier crystallography of a protease-stable domain (reported at 1.9 Å) likewise supports a β-helix + β-sandwich/globular organization consistent with a robust, inextensible fiber tip used for stable anchoring. (raaij2001crystalstructureof pages 1-2)

4.3 Zinc-binding site (trimer stabilization and/or functional surface)

The receptor-binding domain structure contains a Zn2+ ion coordinated octahedrally by six histidines—specifically His445 and His447 from each monomer—forming an unusual metal-binding site at the interface of receptor-binding subdomains. (thomassen2003thestructureof pages 5-7, leiman2010morphogenesisofthe pages 7-8)

4.4 Structural resources (PDB)

A tail morphogenesis review lists gp12 structures corresponding to PDB 1H6W and 1OCY, and the 2003 receptor-binding domain work explicitly associates 1H6W with a gp12 fragment. (thomassen2003thestructureof pages 1-2, leiman2010morphogenesisofthe pages 2-5)

5) Folding, maturation, and pathway context (biogenesis)

5.1 Chaperone-assisted folding (gp57A)

gp12 folding/trimerization is chaperone-dependent: sources describe that gp12 trimers require the chaperone gp57 (gp57A) for folding and proper trimer formation and that full-length gp12 aggregates readily without appropriate assisted folding. (leiman2010morphogenesisofthe pages 7-8, miernikiewicz2016t4phagetail pages 6-7)

This chaperone dependence has practical implications: recombinant production of functional gp12 generally includes co-expression with gp57. (miernikiewicz2016t4phagetail pages 6-7, miernikiewicz2016t4phagetail pages 3-6)

5.2 Infection-stage pathway placement

gp12 is not an enzyme catalyzing a chemical transformation; rather, it is a structural adhesin/RBP acting in the adsorption and entry pathway. The mechanistic pathway is: reversible sampling → baseplate triggering → STF deployment/rotation → stable LPS-core anchoring → tail contraction/genome injection. (mourosi2022understandingbacteriophagetail pages 9-11)

6) Recent developments (prioritized 2023–2024)

6.1 Tail-fiber structure prediction and “structure atlas” approaches (2024)

A 2024 bioRxiv preprint introduces RBPseg, a segmentation/assembly strategy leveraging modern deep-learning structure prediction (ESMFold + AlphaFold2-multimer), and uses T4 as a canonical example with two tail-fiber sets, explicitly noting gp12 STFs as responsible for pseudo-irreversible LPS binding. This exemplifies current trends: integrating predictive models with targeted cryo-EM to build comprehensive tail-fiber structural atlases and to support RBP engineering. (kleinsousa2024towardsacomplete pages 1-4)

6.2 Continued application of the T4 STF/LTF paradigm in contemporary phage-host studies (2023)

A 2023 study of a T-even-like myovirus (CkP1) reiterates the adsorption framework in which irreversible binding is mediated by short tail fibers, while reversible binding by long tail fibers plays a major role in defining host range. This is representative of how T4’s adsorption logic continues to guide interpretation and engineering of related phages. (oliveira2023ckp1bacteriophagea pages 1-2)

7) Current applications and real-world implementations

7.1 Recombinant gp12 as an LPS-binding biologic (anti-inflammatory modulation)

A peer-reviewed 2016 study produced recombinant gp12 (with chaperone gp57), demonstrated it forms trimers and binds LPS in vitro, and tested it in mice as a modulator of LPS-induced inflammation. This is a direct real-world translational direction: using a phage adhesin as a selective LPS-binding/sequestering agent rather than as a whole phage therapeutic. (miernikiewicz2016t4phagetail pages 6-7, miernikiewicz2016t4phagetail pages 3-6)

7.2 Phage engineering and host-range reprogramming (conceptual connection)

Modern RBP-focused engineering emphasizes modularity and the ability to build chimeric RBPs by swapping domains at defined “hotspots.” T4 gp12 is frequently used as a canonical STF reference in discussions of tail-fiber architecture and receptor selection, supporting its relevance as a scaffold or comparative template for host-range engineering (even if gp12 itself is often the secondary-receptor adhesin rather than the primary host-range determinant). (kleinsousa2024towardsacomplete pages 1-4, mourosi2022understandingbacteriophagetail pages 9-11)

7.3 Diagnostics and detection using tail fibers (context)

Contemporary work on tail fibers as receptor binders demonstrates that isolated tail fibers can bind LPS with high affinity and can be proposed as detection reagents. While this is shown in 2023 for another myovirus tail fiber, it reinforces why gp12-like fibers are actively considered for diagnostic capture/decoration strategies: strong, selective binding to conserved bacterial surface glycans. (oliveira2023ckp1bacteriophagea pages 1-2)

8) Expert opinions and analysis (authoritative sources)

8.1 Structural biology perspective: avidity and multivalency

The 2003 JMB receptor-binding domain structure proposes that grooves at the positively charged trimer apex form binding sites for LPS molecules and that multivalent binding (three sites per trimer, many trimers per virion) can explain quasi-irreversible adsorption—an interpretation that remains consistent with contemporary “pseudo-irreversible” language. (thomassen2003thestructureof pages 5-7, kleinsousa2024towardsacomplete pages 1-4)

8.2 Mechanistic infection model perspective

The 2022 IJMS review provides a detailed conformational/mechanical model: after LTF-mediated probing, baseplate switching triggers STF deployment and LPS-core binding, which then aligns the baseplate and triggers downstream contraction and genome ejection. This represents a current synthesis of structural and single-particle observations into an actionable model for engineering receptor usage. (mourosi2022understandingbacteriophagetail pages 9-11)

9) Statistics and quantitative data (from recent/primary studies)

9.1 Structural resolution and stoichiometry

• X-ray crystallography resolutions: 1.9 Å (heat/protease-stable gp12 fragment) and 1.5 Å (receptor-binding domain fragment). (raaij2001crystalstructureof pages 1-2, thomassen2003thestructureof pages 1-2)
• Stoichiometry: gp12 is trimeric, and there are 18 gp12 subunits in the tail (6 trimers). (leiman2010morphogenesisofthe pages 2-5)

9.2 Biophysical binding assay metrics (DLS) for gp12–LPS complex formation

Dynamic light scattering showed gp12 alone ~51 nm, LPS alone ~95.45 nm, and the gp12+LPS mixture forming large complexes averaging ~1980 nm within minutes and stabilizing near ~2000 nm after ~45 min. (miernikiewicz2016t4phagetail pages 3-6)

9.3 In vivo cytokine modulation (mouse LPS challenge)

With LPS challenge (1 mg/kg) and immediate gp12 treatment (100 µg/mouse), serum cytokines were reduced: IL-1α decreased by 72% at 7 h (p=0.002) and IL-6 decreased by 48% at 3 h (p=0.001), with cytokines normalizing by 24 h; histology supported reduced inflammatory infiltrates in multiple organs. (miernikiewicz2016t4phagetail pages 6-7)

10) Summary table (evidence map)

The following table provides a compact, citation-linked map of gp12 functional annotation, evidence type, quantitative data, and recent (2023–2024) developments.

Table: This table summarizes the experimentally supported function, structure, assembly, and application relevance of Enterobacteria phage T4 gene product 12 (gp12), with emphasis on adsorption to LPS and recent 2023-2024 context. It is useful as a compact evidence map for functional annotation and literature-supported reporting.

11) Functional annotation statement (for databases / reports)

Gene 12 (gp12; short tail fiber protein) encodes a trimeric baseplate-anchored adhesin that mediates the irreversible/pseudo-irreversible adsorption step of bacteriophage T4 by binding conserved core regions of host LPS (often described as lipid A–inner core). gp12 fibers are attached to the baseplate via gp10 and stabilized/positioned by gp11. The receptor-binding tip contains a high-resolution characterized, Zn-stabilized knitted trimeric fold (His445/His447 coordination) with a proposed multivalent LPS-binding surface. Folding requires the chaperone gp57A. gp12 acts extracellularly at the phage–bacterium interface during adsorption/entry, and recombinant gp12 retains LPS-binding activity and has been explored as an LPS-sequestering anti-inflammatory modulator in vivo. (mourosi2022understandingbacteriophagetail pages 9-11, hyman2018bacteriophaget4long pages 6-7, thomassen2003thestructureof pages 5-7, miernikiewicz2016t4phagetail pages 6-7)

12) Key URLs and publication dates (selected)

• van Raaij et al. “Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre.” Dec 2001. https://doi.org/10.1006/jmbi.2000.5204 (raaij2001crystalstructureof pages 1-2)
• Thomassen et al. “Structure of the receptor-binding domain of the bacteriophage T4 short tail fibre…” Aug 2003. https://doi.org/10.1016/S0022-2836(03)00755-1 (thomassen2003thestructureof pages 1-2, thomassen2003thestructureof pages 5-7)
• Leiman et al. “Morphogenesis of the T4 tail and tail fibers.” Dec 2010. https://doi.org/10.1186/1743-422X-7-355 (leiman2010morphogenesisofthe pages 2-5)
• Hyman & van Raaij. “Bacteriophage T4 long tail fiber domains.” Dec 2018. https://doi.org/10.1007/s12551-017-0348-5 (hyman2018bacteriophaget4long pages 6-7)
• Mourosi et al. “Understanding bacteriophage tail fiber interaction with host surface receptor…” Oct 2022. https://doi.org/10.3390/ijms232012146 (mourosi2022understandingbacteriophagetail pages 9-11)
• Oliveira et al. “CkP1 bacteriophage…” May 2023. https://doi.org/10.1007/s00253-023-12547-8 (oliveira2023ckp1bacteriophagea pages 1-2)
• Klein-Sousa et al. “Towards a complete phage tail fiber structure atlas.” Oct 2024 (preprint). https://doi.org/10.1101/2024.10.28.620165 (kleinsousa2024towardsacomplete pages 1-4)
• Miernikiewicz et al. “T4 Phage Tail Adhesin Gp12 Counteracts LPS-Induced Inflammation In Vivo.” Jul 2016. https://doi.org/10.3389/fmicb.2016.01112 (miernikiewicz2016t4phagetail pages 6-7, miernikiewicz2016t4phagetail pages 3-6)

References

1. (thomassen2003thestructureof pages 1-2): Ellen Thomassen, Gerrit Gielen, Michael Schütz, Guy Schoehn, Jan Pieter Abrahams, Stefan Miller, and Mark J. van Raaij. The structure of the receptor-binding domain of the bacteriophage t4 short tail fibre reveals a knitted trimeric metal-binding fold. Journal of molecular biology, 331 2:361-73, Aug 2003. URL: https://doi.org/10.1016/s0022-2836(03)00755-1, doi:10.1016/s0022-2836(03)00755-1. This article has 135 citations and is from a domain leading peer-reviewed journal.

2. (raaij2001crystalstructureof pages 1-2): Mark J van Raaij, Guy Schoehn, Martin R Burda, and Stefan Miller. Crystal structure of a heat and protease-stable part of the bacteriophage t4 short tail fibre. Journal of molecular biology, 314 5:1137-46, Dec 2001. URL: https://doi.org/10.1006/jmbi.2000.5204, doi:10.1006/jmbi.2000.5204. This article has 125 citations and is from a domain leading peer-reviewed journal.

3. (leiman2010morphogenesisofthe pages 2-5): Petr G Leiman, Fumio Arisaka, Mark J van Raaij, Victor A Kostyuchenko, Anastasia A Aksyuk, Shuji Kanamaru, and Michael G Rossmann. Morphogenesis of the t4 tail and tail fibers. Virology Journal, 7:355-355, Dec 2010. URL: https://doi.org/10.1186/1743-422x-7-355, doi:10.1186/1743-422x-7-355. This article has 319 citations and is from a peer-reviewed journal.

4. (kleinsousa2024towardsacomplete pages 1-4): Victor Klein-Sousa, Aritz Roa-Eguiara, Claudia S. Kielkopf, Nicholas Sofos, and Nicholas M. I. Taylor. Towards a complete phage tail fiber structure atlas. bioRxiv, Oct 2024. URL: https://doi.org/10.1101/2024.10.28.620165, doi:10.1101/2024.10.28.620165. This article has 2 citations.

5. (mourosi2022understandingbacteriophagetail pages 9-11): Jarin Taslem Mourosi, Ayobami I. Awe, Wenzheng Guo, Himanshu Batra, Harrish Ganesh, Xiaorong Wu, and Jingen Zhu. Understanding bacteriophage tail fiber interaction with host surface receptor: the key “blueprint” for reprogramming phage host range. International Journal of Molecular Sciences, 23:12146, Oct 2022. URL: https://doi.org/10.3390/ijms232012146, doi:10.3390/ijms232012146. This article has 193 citations.

6. (thomassen2003thestructureof pages 5-7): Ellen Thomassen, Gerrit Gielen, Michael Schütz, Guy Schoehn, Jan Pieter Abrahams, Stefan Miller, and Mark J. van Raaij. The structure of the receptor-binding domain of the bacteriophage t4 short tail fibre reveals a knitted trimeric metal-binding fold. Journal of molecular biology, 331 2:361-73, Aug 2003. URL: https://doi.org/10.1016/s0022-2836(03)00755-1, doi:10.1016/s0022-2836(03)00755-1. This article has 135 citations and is from a domain leading peer-reviewed journal.

7. (hyman2018bacteriophaget4long pages 6-7): Paul Hyman and Mark van Raaij. Bacteriophage t4 long tail fiber domains. Biophysical Reviews, 10:463-471, Dec 2018. URL: https://doi.org/10.1007/s12551-017-0348-5, doi:10.1007/s12551-017-0348-5. This article has 64 citations and is from a peer-reviewed journal.

8. (leiman2010morphogenesisofthe pages 7-8): Petr G Leiman, Fumio Arisaka, Mark J van Raaij, Victor A Kostyuchenko, Anastasia A Aksyuk, Shuji Kanamaru, and Michael G Rossmann. Morphogenesis of the t4 tail and tail fibers. Virology Journal, 7:355-355, Dec 2010. URL: https://doi.org/10.1186/1743-422x-7-355, doi:10.1186/1743-422x-7-355. This article has 319 citations and is from a peer-reviewed journal.

9. (miernikiewicz2016t4phagetail pages 6-7): Paulina Miernikiewicz, Anna Kłopot, Ryszard Soluch, Piotr Szkuta, Weronika Kęska, Katarzyna Hodyra-Stefaniak, Agnieszka Konopka, Marcin Nowak, Dorota Lecion, Zuzanna Kaźmierczak, Joanna Majewska, Marek Harhala, Andrzej Górski, and Krystyna Dąbrowska. T4 phage tail adhesin gp12 counteracts lps-induced inflammation in vivo. Frontiers in Microbiology, Jul 2016. URL: https://doi.org/10.3389/fmicb.2016.01112, doi:10.3389/fmicb.2016.01112. This article has 118 citations and is from a peer-reviewed journal.

10. (miernikiewicz2016t4phagetail pages 3-6): Paulina Miernikiewicz, Anna Kłopot, Ryszard Soluch, Piotr Szkuta, Weronika Kęska, Katarzyna Hodyra-Stefaniak, Agnieszka Konopka, Marcin Nowak, Dorota Lecion, Zuzanna Kaźmierczak, Joanna Majewska, Marek Harhala, Andrzej Górski, and Krystyna Dąbrowska. T4 phage tail adhesin gp12 counteracts lps-induced inflammation in vivo. Frontiers in Microbiology, Jul 2016. URL: https://doi.org/10.3389/fmicb.2016.01112, doi:10.3389/fmicb.2016.01112. This article has 118 citations and is from a peer-reviewed journal.

11. (oliveira2023ckp1bacteriophagea pages 1-2): Hugo Oliveira, Sílvio Santos, Diana P. Pires, Dimitri Boeckaerts, Graça Pinto, Rita Domingues, Jennifer Otero, Yves Briers, Rob Lavigne, Mathias Schmelcher, Andreas Dötsch, and Joana Azeredo. Ckp1 bacteriophage, a s16-like myovirus that recognizes citrobacter koseri lipopolysaccharide through its long tail fibers. Applied Microbiology and Biotechnology, 107:3621-3636, May 2023. URL: https://doi.org/10.1007/s00253-023-12547-8, doi:10.1007/s00253-023-12547-8. This article has 4 citations and is from a domain leading peer-reviewed journal.

12. (miernikiewicz2016t4phagetail pages 2-3): Paulina Miernikiewicz, Anna Kłopot, Ryszard Soluch, Piotr Szkuta, Weronika Kęska, Katarzyna Hodyra-Stefaniak, Agnieszka Konopka, Marcin Nowak, Dorota Lecion, Zuzanna Kaźmierczak, Joanna Majewska, Marek Harhala, Andrzej Górski, and Krystyna Dąbrowska. T4 phage tail adhesin gp12 counteracts lps-induced inflammation in vivo. Frontiers in Microbiology, Jul 2016. URL: https://doi.org/10.3389/fmicb.2016.01112, doi:10.3389/fmicb.2016.01112. This article has 118 citations and is from a peer-reviewed journal.

Artifacts

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Citations

1. kleinsousa2024towardsacomplete pages 1-4
2. mourosi2022understandingbacteriophagetail pages 9-11
3. leiman2010morphogenesisofthe pages 2-5
4. raaij2001crystalstructureof pages 1-2
5. thomassen2003thestructureof pages 5-7
6. thomassen2003thestructureof pages 1-2
7. leiman2010morphogenesisofthe pages 7-8
8. https://doi.org/10.3390/ijms232012146;
9. https://doi.org/10.1101/2024.10.28.620165
10. https://doi.org/10.1016/S0022-2836(03
11. https://doi.org/10.1006/jmbi.2000.5204;
12. https://doi.org/10.3390/ijms232012146
13. https://doi.org/10.1007/s12551-017-0348-5;
14. https://doi.org/10.1186/1743-422X-7-355
15. https://doi.org/10.1006/jmbi.2000.5204
16. https://doi.org/10.1186/1743-422X-7-355;
17. https://doi.org/10.3389/fmicb.2016.01112
18. https://doi.org/10.3389/fmicb.2016.01112;
19. https://doi.org/10.1101/2024.10.28.620165;
20. https://doi.org/10.1007/s00253-023-12547-8
21. https://doi.org/10.1007/s12551-017-0348-5
22. https://doi.org/10.1016/s0022-2836(03
23. https://doi.org/10.1006/jmbi.2000.5204,
24. https://doi.org/10.1186/1743-422x-7-355,
25. https://doi.org/10.1101/2024.10.28.620165,
26. https://doi.org/10.3390/ijms232012146,
27. https://doi.org/10.1007/s12551-017-0348-5,
28. https://doi.org/10.3389/fmicb.2016.01112,
29. https://doi.org/10.1007/s00253-023-12547-8,