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ARS Home » Southeast Area » Stoneville, Mississippi » Warmwater Aquaculture Research Unit » Research » Publications at this Location » Publication #223588

Title: Characterization of additional novel immune type receptors in channel catfish, Ictalurus punctatus

Author
item EVENHUIS, J - U. OF MISS. MEDICAL CTR.
item BENGTEN, E - U. OF MISS. MEDICAL CTR.
item SNELL, C - U. OF MISS. MEDICAL CTR.
item Quiniou, Sylvie
item MILLER, N - U. OF MISS. MEDICAL CTR.
item WILSON, M - U. OF MISS. MEDICAL CTR.

Submitted to: Immunogenetics
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/8/2007
Publication Date: 5/30/2007
Citation: Evenhuis, J., Bengten, E., Snell, C., Quiniou, S., Miller, N.W., Wilson, M. 2007. Characterization of additional novel immune type receptors in channel catfish, Ictalurus punctatus. Immunogenetics. 58(8):661-671.

Interpretive Summary: The knowledge of fish immune system is limited. This study relates the discovery of seven new Novel Type Immune Receptors in channel catfish (NITRs) by DNA sequencing. Based on their protein structure, NITRs are potentially functionally akin to mammalian receptors involved in the innate response. This information provides basic information toward a better understanding of the catfish immune system and its role in response to pathogens.

Technical Abstract: Mining of channel catfish (Ictalurus punctatus) expressed sequence tag databases identified seven new novel immune type receptors (IpNITRs). These differed in sequence, but not structure, from previously described IpNITR1-11. IpNITR12a, 12b, 13 and 14, encode proteins containing a single variable (V)-like immunoglobulin (Ig) domain. IpNITR12a and 13 encode a transmembrane (TM) region and cytoplasmic tail (CYT) containing immunoreceptor tyrosine inhibition motifs (ITIMs). IpNITR14 contains a TM and short CYT devoid of signaling motifs and is similar in structure to IpNITR7. IpNITR12b lacks a TM and may represent an IpNITR12a splice variant. In contrast, IpNITR15a, 15b, and 16 encode two Ig domains (V-like domain 1 and V/C2-like domain 2). IpNITR15a and 15b contain TM and CYT with ITIMs. IpNITR16 appears to be a secreted form. The first V-like domains of IpNITR12-16 (except a/b pairs) share 17-32% amino acid identity with each other and with V domains of IpNITR1-11. They therefore represent five additional IpNITR V families (defined as possessing 70% or more amino acid identity). The V/C2 domains of IpNITR15a, 15b and 16 have 94-98% amino acid identity, but share 37-50% amino acid identity with corresponding V/C2 domains found in IpNITR1-4. Phylogenetic analyses indicate IpNITR12-16 are more closely related to other teleost NITRs than to IpNITR1-11. Gene mapping indicates that IpNITRs are linked, and members of the ten known IpNITR families are interspersed. IpNITR12-16 are differentially expressed in various catfish immune-type cells, and preferentially up regulated in PBL by allogeneic stimulation.