Exon–intron structure of outlier tick lipocalins indicate a monophyletic origin within the larger lipocalin family

• Published in: Insect biochemistry and molecular biology Vol. 34; no. 6; pp. 585 - 594
• Main Authors: Mans, Ben J., Neitz, Albert W.H.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.06.2004
• Subjects: Amino Acid Sequence; amino acid sequences; Animals; Argasidae; binding proteins; Carrier Proteins - chemistry; Carrier Proteins - genetics; conserved sequences; exons; Exons - genetics; Female; gene structure; Genes, Insect; histamine binding protein; Insect Proteins - genetics; introns; Introns - genetics; Ixodidae; Lipocalin; Molecular Sequence Data; nucleotide sequences; Ornithodoros savignyi; Phylogeny; protein folding; protein secondary structure; Protein Structure, Secondary; Rhipicephalus appendiculatus; Salivary Glands - chemistry; Salivary Proteins and Peptides - chemistry; Salivary Proteins and Peptides - genetics; Sequence Alignment; sequence homology; structural genes; Tick; ticks; Ticks - chemistry; Ticks - genetics; Toxin; toxins; Toxin; Tick; Ornithodoros savignyi; Lipocalin
• ISSN: 0965-1748; 1879-0240
• DOI: 10.1016/j.ibmb.2004.03.006

All tick proteins assigned to the lipocalin family lack the structural conserved regions (SCRs) that are characteristic of the kernel lipocalins and can thus be classified as outliers. These tick proteins have been assigned to the tick lipocalin family based on database searches that indicated homology between tick sequences and the fact that the histamine binding protein (HBP2) from the hard tick Rhipicephalus appendiculatus (Ixodidae) shows structural similarity to the lipocalin fold. Sequence identity between kernel and outlier lipocalins falls below 20% and the question raised is whether the outlier and kernel lipocalins are truly homologous. More specifically in the case of the tick lipocalins, whether their structural fold is derived from the lipocalin fold or whether convergent evolution resulted in the generation of the basic lipocalin-like fold which consists of an eight stranded continuous anti-parallel β-barrel terminated by a C-terminal α-helix that lies parallel to the barrel. The current study determined the gene structure for HBP2 and TSGP1, TSGP2 and TSGP4, lipocalins identified from the soft tick Ornithodoros savignyi (Argasidae). All tick lipocalins have four introns (A–D) with conserved positions and phases within the tick lipocalin sequence alignment. The positions and phase information are also conserved with regard to the rest of the lipocalin family. Phylogenetic analysis using this information shows conclusively that tick lipocalins are evolutionary related to the rest of the lipocalin family. Tick lipocalins are grouped within a monophyletic clade that indicates a monophyletic origin within the tick lineage and also group with the other arthropod lipocalins in a larger clade. Phylogenetic analysis of sequence alignments based on conserved secondary structure of the lipocalin fold support the conclusions from the gene structure trees. These results indicate that exon–intron arrangement can be useful for the inclusion of outlier lipocalins within the larger lipocalin family.