Molecular Cloning, Sequence, Expression, and Processing of the Interleukin 16 Precursor

Interleukin 16 (IL-16) has been shown to function as chemoattractant factor, as a modulator of T-cell activation, and as an inhibitor of immunodeficiency virus replication. The recent identification of inconsistencies in published IL-16 cDNA nucleotide sequences led to the proposal that IL-16 is syn...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1997-05, Vol.94 (10), p.5273-5277
Main Authors: Baier, Michael, Bannert, Norbert, Werner, Albrecht, Lang, Kurt, Kurth, Reinhard
Format: Article
Language:English
Subjects:
AIDS/HIV
Amino Acid Sequence
Base Sequence
Biological Sciences
Cell lines
Cloning, Molecular
Complementary DNA
COS cells
DNA Primers
DNA, Complementary
Humans
Immunity (Disease)
Interleukin-16 - biosynthesis
Interleukin-16 - chemistry
Interleukin-16 - metabolism
Lymphocytes - immunology
Medical research
Messenger RNA
Molecular Sequence Data
Nucleotides
Open Reading Frames
Polymerase Chain Reaction
Protein precursors
Protein Precursors - biosynthesis
Protein Precursors - chemistry
Protein Precursors - metabolism
Protein Processing, Post-Translational
Proteins
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
RNA
RNA, Messenger - biosynthesis
T lymphocytes
Transcription, Genetic
Untranslated regions
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Summary:Interleukin 16 (IL-16) has been shown to function as chemoattractant factor, as a modulator of T-cell activation, and as an inhibitor of immunodeficiency virus replication. The recent identification of inconsistencies in published IL-16 cDNA nucleotide sequences led to the proposal that IL-16 is synthesized in the form of a large precursor protein (pro-IL-16). To identify the true transcriptional start of the IL-16 mRNA rapid amplification of cDNA ends methods were applied. The complete pro-IL-16 cDNA was subsequently molecularly cloned, sequenced, and expressed in COS-7 cells. We report here that pro-IL-16 is most likely synthesized as a 67-kDa protein and is encoded from a major 2.6-kb transcript. Recombinant pro-IL-16 polypeptides are specifically cleaved in lysates of CD8(+) cells, suggesting that the naturally secreted bioactive form of IL-16 is smaller than the originally published 130 amino acids fragment. Moreover, in contrast to other interleukins such as IL-15, IL-16 mRNA expression is almost exclusively limited to lymphatic tissues underlining the potential of IL-16 as an immune regulatory molecule.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.94.10.5273