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Coronaviruses are a class of virus responsible of the recent outbreak ofHuman Severe Acute Respiratory Syndrome. The molecular machinery behind theviral entry and thus infectivity is based on the formation of the complex ofvirus spike protein with the angiotensin-converting enzyme 2 (ACE2). Thedetection of putative allosteric sites on the viral spike protein can trace thepath to develop allosteric drugs to weaken the strength of the spike-ACE2interface and, thus, reduce the viral infectivity. In this work we presentresults of the application of the Protein Contact Network (PCN) paradigm to thecomplex SARS-CoV spike - ACE2 relative to both 2003 SARS and the recent 2019 -CoV. Results point to a specific region, present in both structures, that ispredicted to act as allosteric site modulating the binding of the spike proteinwith ACE2.

Mapping active allosteric loci SARS-CoV Spike Proteins by means of Protein Contact Networks