Molecular cloning and sequence analysis of interleukin 16 from nonhuman primates and from the mouse

Interleukin 16 (IL-16) is synthesized as a 67 000 Mr precursor (pro-IL-16), but only a carboxy terminal part of 12 000-14 000 Mr is secreted by CD8(+) lymphocytes. This lymphokine binds to CD4 and has been shown to induce migration, affect the activation state of T cells, and inhibit immunodeficienc...

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Published inImmunogenetics (New York) Vol. 47; no. 5; pp. 390 - 397
Main Authors Bannert, N, Adler, H S, Werner, A, Baier, M, Kurth, R
Format Journal Article
LanguageEnglish
Published United States 01.04.1998
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Summary:Interleukin 16 (IL-16) is synthesized as a 67 000 Mr precursor (pro-IL-16), but only a carboxy terminal part of 12 000-14 000 Mr is secreted by CD8(+) lymphocytes. This lymphokine binds to CD4 and has been shown to induce migration, affect the activation state of T cells, and inhibit immunodeficiency virus replication. It has been suggested that CD8(+) cell-derived soluble factors play a pivotal role in protecting natural-host nonhuman primates from developing immunodeficiency following SIV infection. In a first attempt to address this question, we cloned and sequenced the IL-16 cDNA from different primates. Here we report the pro-IL-16 sequence from chimpanzees, African green monkeys (AGM), rhesus macaques, and cynomolgus macaques. In order to compare and analyze structural motifs possibly involved in processing, intracellular targeting, or secretion, we extended our study to the New World monkeys saimiri and aotus and to the mouse. Alignments of deduced amino acids reveal that the human protein shares 99% similarity to that of chimpanzees, approximately 95% to rhesus, cynomolgus and AGM, about 90% to aotus and saimiri, and 77.5% to the mouse. Phylogenetic analyses revealed the expected evolutionary groupings.
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ISSN:0093-7711
1432-1211
DOI:10.1007/s002510050374