Abstract
Despite the huge effort to contain the infection, the novel SARS-CoV-2 coronavirus has rapidly become pandemic, mainly due to its extremely high human-to-human transmission capability, and a surprisingly high viral charge of symptom-less people. While the seek for a vaccine is still ongoing, promising results have been obtained with antiviral compounds. In particular, lactoferrin is regarded to have beneficial effects both in preventing and soothing the infection. Here, we explore the possible molecular mechanisms with which lactoferrin interferes with SARS-CoV-2 cell invasion, preventing attachment and/or entry of the virus. To this aim, we search for possible interactions lactoferrin may have with virus structural proteins and host receptors. Representing the molecular iso-electron surface of proteins in terms of 2D-Zernike descriptors, we 1) identified putative regions on the lactoferrin surface able to bind sialic acid present on the host cell membrane, sheltering the cell from the virus attachment; 2) showed that no significant shape complementarity is present between lactoferrin and the ACE2 receptor, while 3) two high complementarity regions are found on the N- and C-terminal domains of the SARS-CoV-2 spike protein, hinting at a possible competition between lactoferrin and ACE2 for the binding to the spike protein.
Highlights
Lactoferrin (Lf) is a versatile glycoprotein, which plays a key role in many biological functions Redwan et al (2014)
To assess whether lactoferrin could influence the attachment factors, we investigated the ability of Lt to bind to sialic acid (SIA) or heparan sulfate (HS) receptors LangfordSmith et al (2015), both considered involved in SARS-CoV-2 infection Milanetti et al (2020a), Liu et al (2020), Robson (2020), and Vandelli et al (2020), as well as to other coronavirus infections Schwegmann-Weßels and Herrler (2006), Lang et al (2011), Hulswit et al (2019) and Tortorici et al (2019)
Sialoside (SIA) and/or heparan sulfate (HF) chains mediate the attachment of the virion to the cell surface
Summary
Lactoferrin (Lf) is a versatile glycoprotein, which plays a key role in many biological functions Redwan et al (2014). Each lobe possesses a metal-binding site, able to bind iron and other ions like Cu2+, Zn2+, and Mn3+ Baker and Baker (2005) and Giansanti et al (2016) This protein is present in saliva, tears, seminal fluid, white blood cells, and milk of mammals Niaz et al (2019). Despite the name, the iron cargo capacity of Lf is not the prominent activity exerted by this molecule Instead, it performs antioxidant, anti-inflammatory, and anticancer activities Caccavo et al (2002) and Giansanti et al (2016), together with a broad antimicrobial action against bacteria and fungi. The latter activity, in particular, is due to Lf’s ability to reversibly bind two atoms of iron with high
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