How does zinc modify the common cold? Clinical observations and implications regarding mechanisms of action

• Published in: Medical hypotheses Vol. 46; no. 3; pp. 295 - 302
• Main Authors: Novick, S.G., Godfrey, J.C., Godfrey, N.J., Wilder, H.R.
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.03.1996; Elsevier
• Subjects: Biological and medical sciences; Carrier Proteins - physiology; Common Cold - virology; Ent. Stomatology; Humans; Intercellular Adhesion Molecule-1 - physiology; Medical sciences; Models, Chemical; Nasal Mucosa - innervation; Nasal Mucosa - virology; Pharmacology. Drug treatments; Rhinovirus - drug effects; Synaptic Transmission - drug effects; Synaptic Transmission - physiology; Zinc - pharmacology; Infection; Human; Chemotherapy; Treatment; Viral disease; ENT disease; Common cold; Mechanism of action; Zinc
• ISSN: 0306-9877; 1532-2777
• DOI: 10.1016/S0306-9877(96)90259-5

Clinical studies have shown that ionic zinc (Zn 2+) dissolved in the mouth shortened manifestations of the common cold significantly, by an unknown mechanism. The observed immediate effect on symptoms is consonant with osmotic transport of Zn 2+, placing a temporary chemical clamp on critical nerves. It is proposed that transient elevation of Zn 2+ concentration in and around the nasal cavity facilitates Zn 2+ complexation with known intercellular adhesion molecule binding sites on rhinovirus surfaces which prevents rhinovirus binding to cells and interrupts infection. The crystallographically determined surface of rhinovirus-14 has been found to contain binding sites for at least 360 Zn 2+. Such binding of Zn 2+ would be stabilized by numerous histidine, methionine, tyrosine and car☐yl/car☐ylate groups known to line the HRV-14 surface canyons. The resulting blockage of HRV docking with intercellular adhesion molecule binding sites is proposed to be responsible for the observed reduction of the duration of colds by statistically significant and clinically meaningful times.