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Neomycin

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Neomycin
Clinical data
Trade namesNeo-rx
AHFS/Drugs.comMonograph
MedlinePlusa682274
Routes of
administration		Topical, oral
ATC code
Legal status
Legal status
Pharmacokinetic data
Bioavailability< 3% (oral)[1]
Protein binding(Not used systemically)
Metabolism(Not used systemically)
Elimination half-life2 to 3 hours
Identifiers
  • (2RS,3S,4S,5R)-5-Amino-2-(aminomethyl)-6-((2R,3S,4R,5S)-5-((1R,2R,5R,6R)-3,5-diamino-2-((2R,3S,4R,5S)-3-amino-6-(aminomethyl)-4,5-dihydroxytetrahydro-2H-pyran-2-yloxy)-6-hydroxycyclohexyloxy)-4-hydroxy-2-(hydroxymethyl)tetrahydrofuran-3-yloxy)tetrahydro-2H-pyran-3,4-diol
CAS Number
PubChem CID
IUPHAR/BPS
DrugBank
ChemSpider
UNII
KEGG
ChEBI
ChEMBL
ECHA InfoCard100.014.333 Edit this at Wikidata
Chemical and physical data
FormulaC23H46N6O13
Molar mass614.650 g·mol−1
3D model (JSmol)
  • O([C@H]3[C@H](O[C@@H]2O[C@H](CO)[C@@H](O[C@H]1O[C@@H](CN)[C@@H](O)[C@H](O)[C@H]1N)[C@H]2O)[C@@H](O)[C@H](N)C[C@@H]3N)[C@H]4O[C@@H]([C@@H](O)[C@H](O)[C@H]4N)CN
  • InChI=1S/C23H46N6O13/c24-2-7-13(32)15(34)10(28)21(37-7)40-18-6(27)1-5(26)12(31)20(18)42-23-17(36)19(9(4-30)39-23)41-22-11(29)16(35)14(33)8(3-25)38-22/h5-23,30-36H,1-4,24-29H2/t5-,6+,7+,8?,9+,10+,11-,12+,13+,14-,15+,16-,17+,18-,19+,20-,21+,22-,23-/m0/s1 X markN
  • Key:PGBHMTALBVVCIT-DPNHOFNISA-N X markN
 X markNcheckY (what is this?)  (verify)

Neomycin, also known as framycetin, is an aminoglycoside antibiotic that displays bactericidal activity against Gram-negative aerobic bacilli and some anaerobic bacilli where resistance has not yet arisen. It is generally not effective against Gram-positive bacilli and anaerobic Gram-negative bacilli. Neomycin comes in oral and topical formulations, including creams, ointments, and eyedrops. Neomycin belongs to the aminoglycoside class of antibiotics that contain two or more amino sugars connected by glycosidic bonds.

Neomycin was discovered in 1949 by microbiologist Selman Waksman and his student Hubert Lechevalier at Rutgers University. Neomycin received approval for medical use in 1952.[2] Rutgers University was granted the patent for neomycin in 1957.[3]

Discovery

[edit]

Neomycin was discovered in 1949 by the microbiologist Selman Waksman and his student Hubert Lechevalier at Rutgers University. It is produced naturally by the bacterium Streptomyces fradiae.[4] Synthesis requires specific nutrient conditions in either stationary or submerged aerobic conditions. The compound is then isolated and purified from the bacterium.[5]

Medical uses

[edit]

Neomycin is typically applied as a topical preparation, such as Neosporin (neomycin/polymyxin B/bacitracin). In 2023, the topical combination of neomycin with dexamethasone and polymyxin B (neomycin/polymyxin B/hydrocortisone) was the 260th most commonly prescribed medication in the United States, with more than 1 million prescriptions.[6][7]

The antibiotic can also be administered orally, in which case it is usually combined with other antibiotics. Neomycin is very poorly absorbed from the gastrointestinal tract and mostly stays in the gut, exiting with feces. It has been used as a preventive measure for hepatic encephalopathy and hypercholesterolemia. By killing bacteria in the intestinal tract, Neomycin keeps ammonia levels low and prevents hepatic encephalopathy. Orally administered neomycin has also been used to reduce the risk of post operative infection following gastrointestinal surgery and[8] to treat small intestinal bacterial overgrowth.

Neomycin has good activity against Gram-positive and Gram-negative bacteria, but is ototoxic and nephrotoxic (damaging to kidney function) at doses required to inhibit bacteria even when compared to other aminoglycosides.. It is thus not used systemically.[9] Its only use as an injection is when neomycin is included, in small quantities, as a preservative in some vaccines – typically 25 μg per dose.[10]

Spectrum

[edit]

Similar to other aminoglycosides, neomycin has excellent activity against Gram-negative bacteria and is partially effective against Gram-positive bacteria. It is relatively toxic to humans, with allergic reactions noted as a common adverse reaction (see: hypersensitivity).[11] Physicians sometimes recommend using antibiotic ointments without neomycin, such as Polysporin.[12] The following represents minimum inhibitory concentration (MIC) susceptibility data for a few medically significant Gram-negative bacteria.[13]

  • Enterobacter cloacae: >16 μg/ml
  • Escherichia coli: 1 μg/ml
  • Proteus vulgaris: 0.25 μg/ml

Waksman and Lechevalier originally noted that neomycin was active against streptomycin-resistant bacteria as well as Mycobacterium tuberculosis, the causative agent for tuberculosis.[14]

Side effects

[edit]

In 2005–06, Neomycin was the fifth-most-prevalent allergen in patch test results (10.0%).[15] It was named Allergen of the Year in 2010.[16]

Like other aminoglycosides, neomycin has been shown to be ototoxic, causing tinnitus, hearing loss, and vestibular problems in a small number of patients. Neomycin affects the cochlea, which is found in the inner ear.[17] Hearing loss is caused by ear hair cell death, which occurs in response to treatment with neomycin. Routes known to lead to ototoxicity include rectal, parenteral, intrapleural, topical, and oral.[17] Although cases of ototoxicity via the oral route are most commonly associated gastrointestinal inflammation or renal impairment, there have been cases where people with normal function in these organs developed ototoxicity after prolonged use.[17] Patients with existing tinnitus or sensorineural hearing loss are advised to speak with a healthcare practitioner about the risks and side effects prior to taking this medication.[citation needed]

Neomycin is also a known GABA gamma-Aminobutyric acid antagonist and can be responsible for seizures and psychosis, at least in animal models.[18]

Mechanism of action

[edit]

Activity

[edit]

Neomycin's antibacterial activity stems from its binding to the 30S subunit of the prokaryotic ribosome, where it inhibits prokaryotic translation of mRNA.[19]

Neomycin also exhibits a high binding affinity for phosphatidylinositol 4,5-bisphosphate (PIP2), a phospholipid component of cell membranes.[20]

Resistance

[edit]

Neomycin resistance is most commonly conferred by a kanamycin kinase gene; the resultant enzyme inactivates the antibiotic by attaching a phosphate group. This gene is variously known as APH (aminoglycoside 3' phosphotransferase) or neo. Currently, research is being performed to understand if derivatives of neomycin can have the same antibiotic effects while still being effective against neomycin-resistant bacteria.[21] Other neomycin-inactivating enzymes also exist.[22]

Specific versions of the neo gene are commonly included in DNA plasmids used to establish stable mammalian cell lines expressing cloned proteins in culture. Although neomycin does not disrupt the eukaryotic ribosome, the related G418 inhibits both prokaryotic and eukaryotic ribosomes and is inactivated by APH/neo. As a result, G418 makes neo a selectable marker usable in both eukaryotes and prokaryotes: by adding it to a cell culture, cells not expressing the marker are killed.[23] Many commercially available protein expression plasmids use this approach.

Chemistry

[edit]

Composition

[edit]

Pharmaceutical grade neomycin is composed of several related compounds including neomycin A, neomycin B, neomycin C, and a few minor compounds found in much lower quantities. Neomycin B is the most active component in neomycin followed by neomycin C, which is about half as active.[24] Neomycin A is an inactive degradation product of the C and B isomers.[25] The quantities of these components in neomycin vary from lot-to-lot depending on the manufacturer and manufacturing process.[26]

Neomycin was first isolated from the Streptomyces fradiae and Streptomyces albogriseus in 1949 (NBRC 12773).[27] This original isolation consists of a mixture of neomycin B (framycetin); and its epimer neomycin C, the latter component accounting for some 5–15% of the mixture.[14]

Structure

[edit]

The inactive neomycin A (neamine) consists of two ring moities, both derived from glucose: 2-deoxystreptamine (ring I) and D-neosamine (ring II).[28] Ring I is linked to ring II via a 1→4 glycoside linkage.[29]

Neomycin B and C are 23-carbon molecules with a four-ring structure. Three of the rings are six-membered, and one is five-membered. Neomycin C are stereoisomers of each other and differ by only one stereocenter (C-5‴), one giving the R conformation and the other giving the S conformation.[30] The four rings, from I to IV, of neomycin B (framycetin) are 2-deoxystreptamine (2-DOS), D-neosamine, D-ribose, and L-neosamine. The rings are attached in a II-I-III-IV pattern,[28] specifically using linkages of 1→3 and 1→5 between IV, III, and II and a 1→4 linkage between I and II.[30] Neomycin differs by a flip of the neosamine ring IV, which it has in the original D configuration.[28]

Properties

[edit]

Neomycin was described as thermostable and soluble in water (while insoluble in organic solvents) by its discoverers. It is a basic compound that is most active with an alkaline reaction.[14]

Biosynthetic pathway

[edit]
Neomycin B biosynthesis

The biosynthetic gene cluster for neomycin in Streptomyces fradiae has been sequenced and largely analyzed. In broad strokes, the biosynthesis involves:[28]

  1. Production of 2-deoxystreptamine from glucose-6-phosphate;
  2. Production of the two-ringed 2′-N-acetylparomamine from 2-deoxystreptamine and UDP-N-acetylglucosamine, followed by its modification into neamine (neomycin A);
  3. Addition of a ribose group onto neomycin A, plus further modifications to arrive at ribostamycin;
  4. Addition of another UDP-N-acetylglucosamine to form the initial four-ringed 6‴-deamino-6‴hydroxyneomyxin, followed by its modification into neomycin C, which is then epimerized into neomycin B.

Three genes that code for enzymes are responsible for the first stepL: (in the order of their action) 2-deoxy-scyllo-inosose synthase (btr/neoC, neo7); a 2-deoxy-scyllo-inosamine dehydrogenase (btr/neoE, neo5); and a L-glutamine:2-deoxy-scyllo-inosose aminotransferase (btr/neoS, neoB, neo6).[31][28] (In newer literature, the genes are named by neoX instead of btrX with the same letter. The btr designation was inherited from analysis of butirosin biosynthesis, which had homologous genes and served as a basis for the analysis of neomycin biosynthetic genes – one that should not have been directly applied onto the neomycin cluster.[32] There is, however, yet another neoX designation that uses an indepedent lettering scheme used by UniProt.)[33]

The second step uses a 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase (btr/neoM, neo8; UniProt "neoD") for the initial coupling, followed by a 2'-N-acetylparomamine deacetylase (btr/neoD, neo16; "neoL"), a flavoprotein paromamine 6'-oxidase (btr/neoQ, neo11; "neoG"), and a neamine transaminase (btrB, neo18; "neoN").[28][31]

The third step is the attachment of the D-ribose via ribosylation of neamine, using 5-phosphoribosyl-1-diphosphate (PRPP) as the ribosyl donor (BtrL, BtrP).[34] This is catalyzed by a UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase (btr/neoF, Neo15; "neoK").[35]

The final steps are for the production of neomycins B and C from ribostamycin.[36] Production of the latter from ribostamycin was accomplished using recombinant enzymes in 2009, providing proof for most of the hypothsized pathway.[37] The pathway starts with again neo8 to add the ring, neo16, neo11, and neo18 to convert it to a neosamine, making at this point neomycin C.[28] The SAM-dependent neomycin C epimerase (neoN, "neoH") then converts neomycin C into neomycin B.[32]

Genetic manipulation has been used to improve the efficacy of the epimerization step in order to produce a product with higher neomycin B concentration. The epimerization enzyme resides on a different gene cluster, along with a regulatory gene and an enzyme that produces SAM.[32]

Additional activities

[edit]

DNA binding

[edit]

Aminoglycosides such as neomycin are known for their ability to bind to duplex RNA with high affinity in vitro.[38] The association constant for neomycin with A-site RNA is in the 109 M−1 range.[39] However, more than 50 years after its discovery, its DNA-binding properties were still unknown. Neomycin has been shown to induce thermal stabilization of triplex DNA, while having little or almost no effect on the B-DNA duplex stabilization.[40] Neomycin was also shown to bind to structures that adopt an A-form structure, triplex DNA being one of them. Neomycin also includes DNA:RNA hybrid triplex formation.[41]

Immunostimulation

[edit]

In 2018, scientists from Yale University found that topical application of aminoglycosides to the mucosa of lab animals increased their ability to resist future challenges by herpes simplex viruses, influenza A virus and Zika virus. Neomycin was one of the more effective aminoglycosides. The authors found that this effect had nothing to do with the local microbiome; instead, aminoglycosides induced interferon-stimulated genes in a way that requires TLR3, TICAM1, IRF3, and IRF7. A reduction in viral replication was also reported in human cell cultures.[42][43]

An 2024 paper reports additional results from animal experiments. It appears that neomycin not only prevents various viral infections in rodents, but is also useful as a treatment. The paper also reported on a very small human randomized controlled trial where Neosporin was applied into their nostrils and the ISG expression was measured. Although a significant increase in ISGs were seen in the volunteers on average, the increase was very inconsistent from person to person.[44]

References

[edit]
  1. ↑ Kunin CM, Chalmers TC, Leevy CM, Sebastyen SC, Lieber CS, Finland M (February 1960). "Absorption of orally administered neomycin and kanamycin; with special reference to patients with severe hepatic and renal disease". The New England Journal of Medicine. 262 (8): 380–385. doi:10.1056/NEJM196002252620802. PMID 14412744.
  2. ↑ Fischer J, Ganellin CR (2006). Analogue-based Drug Discovery. John Wiley & Sons. p. 507. ISBN 978-3-527-60749-5. Archived from the original on 1 August 2020. Retrieved 25 May 2020.
  3. ↑ US 2799620, Waksman SA, Lechevalier HA, "Neomycin and process of preparation", published 16 July 1957, issued 18 July 1957, assigned to Rutgers Research and Educational Foundation.
  4. ↑ "The Nobel Prize in Physiology or Medicine 1952". NobelPrize.org. Nobel Foundation. Archived from the original on 19 June 2018. Retrieved 29 October 2008.
  5. ↑ "Neomycin". Pharmaceutical Manufacturing Encyclopedia. Vol. 3 (3rd ed.). 2007. pp. 2415–2416.
  6. ↑ Kane SP. "The Top 300 of 2023". ClinCalc. Archived from the original on 17 August 2025. Retrieved 17 August 2025.
  7. ↑ Kane SP. "Dexamethasone; Neomycin; Polymyxin B Drug Usage Statistics, United States, 2014 - 2023". ClinCalc. Retrieved 17 August 2025.
  8. ↑ Lewis RT (June 2002). "Oral versus systemic antibiotic prophylaxis in elective colon surgery: a randomized study and meta-analysis send a message from the 1990s". Canadian Journal of Surgery. Journal Canadien De Chirurgie. 45 (3): 173–180. PMC 3686946. PMID 12067168.
  9. ↑ Dewick M (March 2009). Medicinal natural products: a biosynthetic approach (3rd ed.). The Atrium, Southern Gate, Chichester, West Sussex, United Kingdom: John Wiley and Sons Ltd. pp. 508, 510, 511. ISBN 978-0-470-74168-9.
  10. ↑ Heidary N, Cohen DE (September 2005). "Hypersensitivity reactions to vaccine components". Dermatitis. 16 (3): 115–120. doi:10.1097/01206501-200509000-00004. PMID 16242081. S2CID 31248441.
  11. ↑ DermNet dermatitis/neomycin-allergy
  12. ↑ "Your Medicine Cabinet". DERMAdoctor.com, Inc. Archived from the original on 9 July 2009. Retrieved 19 October 2008.
  13. ↑ "Neomycin sulfate, EP Susceptibility and Minimum Inhibitory Concentration (MIC) Data" (PDF). TOKU-E. Archived (PDF) from the original on 22 December 2015. Retrieved 31 March 2014.
  14. 1 2 3 Waksman SA, Lechevalier HA (March 1949). "Neomycin, a New Antibiotic Active against Streptomycin-Resistant Bacteria, including Tuberculosis Organisms". Science. 109 (2830). New York, N.Y.: 305–307. Bibcode:1949Sci...109..305W. doi:10.1126/science.109.2830.305. PMID 17782716.
  15. ↑ Zug KA, Warshaw EM, Fowler JF, Maibach HI, Belsito DL, Pratt MD, et al. (2009). "Patch-test results of the North American Contact Dermatitis Group 2005-2006". Dermatitis. 20 (3): 149–160. doi:10.2310/6620.2009.08097. PMID 19470301. S2CID 24088485.
  16. ↑ McNamara, Damian. (2010). Neomycin Is Named Contact Allergen of the Year Deprecated link archived 22 April 2015 at archive.today
  17. 1 2 3 Langman, A. Neomycin ototoxicity. Otolaryngology Head and Neck Surgery 1994, 110, 441-444.
  18. ↑ Lee C, de Silva AJ (March 1979). "Interaction of neuromuscular blocking effects of neomycin and polymyxin B". Anesthesiology. 50 (3): 218–220. doi:10.1097/00000542-197903000-00010. PMID 219730. S2CID 13551808.
  19. ↑ Mehta R, Champney WS (September 2003). "Neomycin and paromomycin inhibit 30S ribosomal subunit assembly in Staphylococcus aureus". Current Microbiology. 47 (3): 237–243. doi:10.1007/s00284-002-3945-9. PMID 14570276. S2CID 23170091.
  20. ↑ Gabev E, Kasianowicz J, Abbott T, McLaughlin S (February 1989). "Binding of neomycin to phosphatidylinositol 4,5-bisphosphate (PIP2)". Biochimica et Biophysica Acta (BBA) - Biomembranes. 979 (1): 105–112. doi:10.1016/0005-2736(89)90529-4. PMID 2537103.
  21. ↑ Bera, S.; Zhanel, G.; Schweizer, F. Design, Synthesis, and Antibacterial Activities of Neomycin−Lipid Conjugates: Polycationic Lipids with Potent Gram-Positive Activity | Journal of Medicinal Chemistry. Journal of Medicinal Chemistry 2003, 51, 6160-6164.
  22. ↑ Ramirez MS, Tolmasky ME (December 2010). "Aminoglycoside modifying enzymes". Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy. 13 (6): 151–171. doi:10.1016/j.drup.2010.08.003. PMC 2992599. PMID 20833577.
  23. ↑ "G418/neomycin-cross resistance?". Archived from the original on 25 June 2009. Retrieved 19 October 2008.
  24. ↑ "NCI EVS Explore: Neomycin C (C95127)". evsexplore.semantics.cancer.gov.
  25. ↑ Cammack R, Attwood TK, Campbell PN, Parish JH, Smith AD, Stirling JL, et al. (2006). "neomycin". Oxford Dictionary of Biochemistry and Molecular Biology (2nd ed.). Oxford University Press. p. 453.
  26. ↑ Tsuji K, Robertson JH, Baas R, McInnis DJ (September 1969). "Comparative study of responses to neomycins B and C by microbiological and gas-liquid chromatographic assay methods". Applied Microbiology. 18 (3): 396–398. doi:10.1128/AEM.18.3.396-398.1969. PMC 377991. PMID 4907002.
  27. ↑ Waksman SA, Lechevalier HA, Harris DA (September 1949). "Neomycin—Production and Antibiotic Properties 123". The Journal of Clinical Investigation. 28 (5 Pt 1): 934–939. doi:10.1172/JCI102182. PMC 438928. PMID 16695766.
  28. 1 2 3 4 5 6 7 Huang F, Spiteller D, Koorbanally NA, Li Y, Llewellyn NM, Spencer JB (February 2007). "Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin". Chembiochem. 8 (3): 283–288. doi:10.1002/cbic.200600371. PMID 17206729.
  29. ↑ "UNII - 5981U00LY0 | UNII Search Service". precision.fda.gov. O-2,6-DIAMINO-2,6-DIDEOXY-.ALPHA.-D-GLUCOPYRANOSYL-(1->4)-1,3-DIAMINO-1,2,3-TRIDEOXY-D-MYO-INOSITOL; D-STREPTAMINE, 2-DEOXY-4-O-(2,6-DIAMINO-2,6-DIDEOXY-.ALPHA.-D-GLUCOPYRANOSYL)-
  30. 1 2 PubChem. "Neomycin". PubChem. D-Streptamine, O-2,6-diamino-2,6-dideoxy-.beta.-L-idopyranosyl-(1.->3)-O-.beta.-D-ribofuranosyl-(1->5)]-O-[2,6-diamino-2,6-dideoxy-.alpha.-D-glucopyranosyl-(1->4)]-2-deoxy (synonym from FDA)
  31. 1 2 Kudo F, Yamamoto Y, Yokoyama K, Eguchi T, Kakinuma K (December 2005). "Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773". The Journal of Antibiotics. 58 (12). Tokyo: 766–774. doi:10.1038/ja.2005.104. PMID 16506694.
  32. 1 2 3 Zheng J, Li Y, Guan H, Li J, Li D, Zhang J, et al. (September 2020). "Component Optimization of Neomycin Biosynthesis via the Reconstitution of a Combinatorial Mini-Gene-Cluster in Streptomyces fradiae". ACS Synthetic Biology. 9 (9): 2493–2501. doi:10.1021/acssynbio.0c00281. PMID 32864952.
  33. ↑ "UniProt Q53U18". UniProt.
  34. ↑ Kudo F, Fujii T, Kinoshita S, Eguchi T (July 2007). "Unique O-ribosylation in the biosynthesis of butirosin". Bioorganic & Medicinal Chemistry. 15 (13): 4360–4368. doi:10.1016/j.bmc.2007.04.040. PMID 17482823.
  35. ↑ Fan Q, Huang F, Leadlay PF, Spencer JB (September 2008). "The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: genetic and biochemical evidence for the roles of two glycosyltransferases and a deacetylase". Organic & Biomolecular Chemistry. 6 (18): 3306–3314. doi:10.1039/B808734B. PMID 18802637. S2CID 29942953.
  36. ↑ Llewellyn NM, Spencer JB (December 2006). "Biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics". Natural Product Reports. 23 (6): 864–874. doi:10.1039/B604709M. PMID 17119636.
  37. ↑ Kudo F, Kawashima T, Yokoyama K, Eguchi T (November 2009). "Enzymatic preparation of neomycin C from ribostamycin". The Journal of Antibiotics. 62 (11). Tokyo: 643–646. doi:10.1038/ja.2009.88. PMID 19713992.
  38. ↑ Jin Y, Watkins D, Degtyareva NN, Green KD, Spano MN, Garneau-Tsodikova S, et al. (January 2016). "Arginine-linked neomycin B dimers: synthesis, rRNA binding, and resistance enzyme activity". MedChemComm. 7 (1): 164–169. doi:10.1039/C5MD00427F. PMC 4722958. PMID 26811742.
  39. ↑ Kaul M, Pilch DS (June 2002). "Thermodynamics of aminoglycoside-rRNA recognition: the binding of neomycin-class aminoglycosides to the A site of 16S rRNA". Biochemistry. 41 (24): 7695–7706. doi:10.1021/bi020130f. PMID 12056901.
  40. ↑ Arya DP, Coffee RL (September 2000). "DNA triple helix stabilization by aminoglycoside antibiotics". Bioorganic & Medicinal Chemistry Letters. 10 (17): 1897–1899. doi:10.1016/S0960-894X(00)00372-3. PMID 10987412.
  41. ↑ Arya DP, Coffee RL, Charles I (November 2001). "Neomycin-induced hybrid triplex formation". Journal of the American Chemical Society. 123 (44): 11093–11094. Bibcode:2001JAChS.12311093A. doi:10.1021/ja016481j. PMID 11686727.
  42. ↑ Gopinath S, Kim MV, Rakib T, Wong PW, van Zandt M, Barry NA, et al. (May 2018). "Topical application of aminoglycoside antibiotics enhances host resistance to viral infections in a microbiota-independent manner". Nature Microbiology. 3 (5): 611–621. doi:10.1038/s41564-018-0138-2. PMC 5918160. PMID 29632368.
  43. ↑ "Study: Topical antibiotic triggers unexpected antiviral response | Yale News". Yale News. 9 April 2018.
  44. ↑ Mao T, Kim J, Peña-Hernández MA, Valle G, Moriyama M, Luyten S, et al. (April 2024). "Intranasal neomycin evokes broad-spectrum antiviral immunity in the upper respiratory tract". Proceedings of the National Academy of Sciences of the United States of America. 121 (18) e2319566121. doi:10.1073/pnas.2319566121. PMC 11067057. PMID 38648490.
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