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Abstract: Cathelicidins, antimicrobial peptides with broad spectrum activity, have been almost exclusively found in mammals. Here, we report the cloning of a novel avian cathelicidin, chicken myeloid antimicrobial peptide 27 (CMAP27) from chicken bone marrow cells. A combined expressed sequence tag (EST) and genomic based search revealed a cathelicidin-like gene located at the terminus of chromosome 2. Reverse transcriptase-polymerase chain reaction (RT-PCR) and 5′RACE techniques resulted in a 154 amino acid prepropeptide, homologous to chicken cathelicidin 1 (51%) and most similar to α-helical myeloid antibacterial peptides (MAPs; 29–33%). A putative elastase cleavage site (LVQRG↓RF) suggests the production of a 27 amino acid antimicrobial peptide, predicted to adopt an α-helical configuration followed by a hydrophobic tail. Comparative analyses between antimicrobial peptide domains showed marked similarity between CMAP27 and MAP members of the bovidae family, but not with the α-helical chicken cathelicidin 1. Strongest expression of CMAP27 mRNA was found in myeloid/lymphoid tissues, testis and uropygial gland. In accordance with the phylogenetic tree analysis, these findings support the theory of a common ancestral cathelicidin gene and suggest an important role for cathelicidins in chicken innate host defense. [Copyright &y& Elsevier]

Abstract: Collectins are members of the family of vertebrate C-type lectins. They have been found almost exclusively in mammals, with the exception of chicken MBL. Because of their important role in innate immunity, we sought to identify other collectins in chicken. Using the amino acid sequences of known collectins, the EST database was searched and related to the chicken genome. Three chicken collectins were found and designated chicken Collectin 1 (cCL-1), chicken Collectin 2 (cCL-2), and chicken Collectin 3 (cCL-3), which resemble the mammalian proteins Collectin Liver 1, Collectin 11 and Collectin Placenta 1, respectively. Additionally, a lectin was found which resembled Surfactant Protein A, but lacked the collagen domain. Therefore, it was named chicken Lung Lectin (cLL). Tissue distribution analysis showed cCL-1, cCL-2 and cCL-3 are expressed in a wide range of tissues throughout the digestive, the reproductive and the lymphatic system. Similar to SP-A, cLL is mainly localized in lung tissue. Phylogenetic analysis indicates that cCL-1, cCL-2 and cCL-3 represent new subgroups within the collectin family. The newly found collectins may have an important function in avian host defence. Elucidation of the role of these pattern-recognition molecules could lead to strategies that thwart infectious diseases in poultry, which could also be beneficial for public health. [Copyright &y& Elsevier]