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How Glycosylation Affects PTX3 Functions in Innate Immunity and Inflammation

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How Glycosylation Affects PTX3 Functions in Innate Immunity and Inflammation REVIEW ARTICLE published: 07 January 2013 doi: 10.3389/fimmu.2012.00407 The “sweet” side of a long pentraxin: how glycosylation affects PTX3 functions in innate immunity and inflammation Antonio Inforzato1, Patrick C. Reading 2,3, Elisa Barbati 1, Barbara Bottazzi 1, Cecilia Garlanda1* and Alberto Mantovani 1,4 1 Department of Immunology and Inflammation, Humanitas Clinical and Research Center, Rozzano, Italy 2 Department of Microbiology and Immunology, University of Melbourne, Melbourne, VIC, Australia 3 Victorian Infectious Diseases Reference Laboratory, World Health Organization Collaborating Centre for Reference and Research on Influenza, Melbourne, VIC, Australia 4 Department of Medical Biotechnology and Translational Medicine, University of Milan, Milan, Italy Edited by: Innate immunity represents the first line of defense against pathogens and plays key roles Paul A. Ramsland, Burnet Institute, in activation and orientation of the adaptive immune response. The innate immune system Australia comprises both a cellular and a humoral arm. Components of the humoral arm include sol- Reviewed by: uble pattern recognition molecules (PRMs) that recognize pathogen-associated molecular Andrew T. Hutchinson, University of Technology, Sydney, Australia patterns and initiate the immune response in coordination with the cellular arm, therefore Gregory W. Moseley, Monash acting as functional ancestors of antibodies.The long pentraxin PTX3 is a prototypic soluble University, Australia PRM that is produced at sites of infection and inflammation by both somatic and immune *Correspondence: cells. Gene targeting of this evolutionarily conserved protein has revealed a non-redundant Cecilia Garlanda, Department of role in resistance to selected pathogens. Moreover, PTX3 exerts important functions at Immunology and Inflammation, Humanitas Clinical and Research the crossroad between innate immunity, inflammation, and female fertility. The human Center, Via Manzoni 56, 20089 PTX3 protein contains a single N-glycosylation site that is fully occupied by complex type Rozzano, Milan, Italy. oligosaccharides, mainly fucosylated and sialylated biantennary glycans. Glycosylation has e-mail: cecilia.garlanda@ humanitasresearch.it been implicated in a number of PTX3 activities, including neutralization of influenza viruses, View metadata, citation and similar papers at core.ac.uk modulation of the complement system, and attenuation of leukocyte recruitment. There- brought to you by CORE fore, this post translational modification might act as a fine tuner of PTX3 functions in native provided by Frontiers - Publisher Connector immunity and inflammation. Here we review the studies on PTX3, with emphasis on the glycan-dependent mechanisms underlying pathogen recognition and crosstalk with other components of the innate immune system. Keywords: pathogen recognition, inflammation, glycosylation, pentraxins, PTX3 INTRODUCTION Kooyk and Rabinovich, 2008). In addition, most PRMs are glyco- The innate immune system has evolved to specifically recognize proteins whose glycosidic moiety might have a dramatic impact on and eradicate potentially harmful microorganisms, thus provid- protein targeting and activity. For instance, some toll-like receptors ing the first line of defense against pathogens. Evolutionarily older (TLRs), such as TLR2 and TLR4, require glycosylation for correct than the adaptive immune system, innate immunity plays key roles cell compartmentalization (da Silva Correia and Ulevitch, 2002; in activation and orientation of adaptive immunity that provides Weber et al., 2004), and inhibition of glycosylation prevents TLR3- the immunological memory. Components of the innate immune induced NF-κB activation, although it does not affect expression system that are involved in pathogen recognition and initiation of and trafficking of this receptor (Sun et al., 2006). the immune response are germline-encoded receptors known as Considering cellular localization and function, PRMs are clas- pattern recognition molecules (PRMs). These receptors recognize sified into two major groups: (i) cell-associated receptors, which microbes or microbial moieties collectively named pathogen- are localized in different cellular compartments and include associated molecular patterns (PAMPs; Iwasaki and Medzhitov, endocytic receptors, such as scavenger receptors (Murphy et al., 2010). PRMs can also sense endogenous ligands termed “danger- 2005), signaling receptors, such as TLRs (Akira et al., 2006) and associated molecular patterns (DAMPs),” which are released by nucleotide-binding oligomerization domain (NOD)-like recep- host cells upon tissue damage during, for example, infection, tors (NLR; Meylan et al., 2006), and (ii) fluid phase molecules inflammation, and tumor growth (Matzinger, 2002). As numer- or opsonins, which represent the functional ancestors of anti- ous PAMPs and DAMPs are glycans themselves or accommodate bodies and are involved in pathogen opsonization, complement glycan structures, PRMs are mostly comprised of glycan-binding activation, and self versus modified-self discrimination (Bot- proteins or lectins. These include C-type lectins, siglecs, and tazzi et al., 2010). Fluid phase PRMs are essential effectors and galectins, which contain one or more carbohydrate-recognition modulators of the innate resistance in animals and humans, and domains (CRDs) that are responsible for sugar recognition (van form a heterogeneous group of molecules that includes collectins, www.frontiersin.org January 2013 | Volume 3 | Article 407 | 1 “fimmu-03-00407” — 2013/1/4 — 18:24 — page1—#1 Inforzato et al. PTX3 and glycosylation ficolins, and pentraxins (Fujita, 2002; Holmskov et al., 2003; produced by hepatocytes, where the pro-inflammatory cytokine Bottazzi et al., 2006). IL-6 is a major inducer of CRP both on its own and in synergy Conserved in evolution from arachnids to humans, pentraxins with IL-1 (Pepys and Hirschfield, 2003). are pivotal components of the humoral arm of innate immunity Short pentraxins are important players in humoral innate with a distinctive multimeric structure. Based on the primary immunity, where they have been described to recognize a num- structure of the composing protomers, pentraxins are divided into ber of diverse ligands, mostly in a calcium-dependent manner. two groups: short and long pentraxins (Deban et al., 2011). C- As mentioned above, the first reported ligand of CRP is the C- reactive protein (CRP) and serum amyloid P component (SAP) polysaccharide of Streptococcus pneumoniae. This interaction is are prototypic short pentraxins, whereas pentraxin 3 (PTX3) mediated by phosphorylcholine (PC), a major constituent of the and other subsequently identified proteins represent the long C-type capsule polysaccharides (Tillet and Francis, 1930; Aber- pentraxin arm of the family (Garlanda et al., 2005). nethy and Avery, 1941). CRP recognizes additional pathogens, Here we review past and present literature on this family of including fungi, yeasts, and bacteria, thus promoting phagocyto- proteins, with major emphasis on the long pentraxin PTX3 and sis and resistance to infection (Szalai, 2002). Consistent with this, the glycan-dependent mechanisms underlying its functions in CRP transgenic (Tg) mice are resistant to infection with Strep- pathogen recognition and crosstalk with other components of the tococcus pneumoniae, displaying longer survival time and lower innate immune system. mortality rate than normal littermates (Szalai et al., 1995). SAP is a calcium-dependent lectin originally purified based on its THE SHORT PENTRAXINS binding to the agarose component 4,6-cyclin pyruvate acetal of Pentraxins are distinctively characterized by the presence in their β-D-galactose (Hind et al., 1984). Like CRP, SAP binds a number carboxy-terminal region of a ∼200 amino acid domain containing of bacteria, such as Streptococcus pyogenes and Neisseria meningi- a highly conserved motif of primary sequence known as pentraxin tidis (Hind et al., 1985; Noursadeghi et al., 2000). In addition it has signature (HxCxS/TWxS, where x is any amino acid). In the 1930s, been shown that SAP acts as β inhibitor against influenza virus, CRP was the first purified PRM, which was named after its ability binding in a calcium-dependent fashion to mannose-rich glycans to bind in a calcium-dependent fashion the C-polysaccharide of on the viral hemagglutinin (HA) to inhibit both hemagglutination Streptococcus pneumoniae (Tillet and Francis, 1930; Abernethy and and viral infectivity (Andersen et al., 1997; Horvath et al., 2001). Avery, 1941). Human SAP was subsequently identified as a closely Furthermore, SAP has been described to prevent lipopolysaccha- related protein (i.e., with 51% sequence identity to human CRP; ride (LPS)-mediated complement activation and LPS toxicity (de Emsley et al., 1994). Orthologous proteins to human CRP and Haas et al., 1998, 2000; Noursadeghi et al., 2000). However, the SAP have also been described in the hemolymph of the arthropod relationship between ligand binding and function of these pro- Limulus polyphemus, where they are involved in recognition and teins is still a matter of debate (Noursadeghi et al., 2000; Szalai killing of pathogens (Liu et al., 1982; Armstrong et al., 1996; Shrive et al., 2000; Suresh et al., 2007). et al., 1999). The short pentraxins participate in activation and regulation Both short pentraxins are 25 kDa proteins with a common of the three complement pathways (i.e., classical, lectin, and alter- structural organization that comprises 5
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