Surfactant proteins A and D: trimerized innate immunity proteins with an affinity for viral fusion proteins

Abstract

Innate recognition of viruses is an essential part of the immune response to viral pathogens. This is integral to the maintenance of healthy lungs, which are free from infection and efficient at gaseous exchange. An important component of innate immunity in identifying viruses is the family of C-type collagen containing lectins, also known as collectins. These secreted, soluble proteins are pattern recognition receptors (PRRs) which recognise pathogen-associated molecular patterns (PAMPs), including viral glycoproteins. These innate immune proteins are composed of trimerized units which oligomerise into higher-order structures and facilitate clearance of viral pathogens through multiple mechanisms. Similarly, many viral surface proteins form trimeric configurations, despite not showing primary protein sequence similarities across virus classes and families they belong to. In this review, we discuss the role of lung collectins surfactant proteins A and D (SP-A and SP-D) in viral recognition. Particularly, we focus on the structural similarity and complementarity of these trimeric collectins with the trimeric viral fusion proteins with which, we hypothesise, they have elegantly co-evolved. Recombinant versions of these innate immune proteins may have therapeutic potential in a range of infectious and inflammatory lung diseases including as anti-viral therapeutics.

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Identifiers

ORCID for Chris-Kriton Skylaris: orcid.org/0000-0003-0258-3433

ORCID for Jens Madsen: orcid.org/0000-0003-1664-7645

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