Biomaterial Database

Identification and properties of chlamydial polypeptides that bind eucaryotic cell surface components. 1986

T Hackstadt

An electroblotting technique was used to identify proteins of Chlamydia that bound surface-radioiodinated and Triton X-100-solubilized HeLa cell extracts. Two proteins, with apparent molecular masses of 18 and 32 kilodaltons (kDa), that bound HeLa cell surface components were identified on Chlamydia trachomatis L2 elementary bodies (EBs). Radioiodinated heparin, which disrupts chlamydial association with cultured cells, was also bound by these proteins. These two proteins were found on EBs but were absent or were present in reduced amounts on the noninfectious reticulate bodies. All C. trachomatis strains tested displayed two such proteins, although the apparent molecular weight of the larger protein varied with serotype in correlation with biotype and the disease that it caused. Two Chlamydia psittaci strains examined displayed only a single binding protein in the range of 17 to 19 kDa. All of the binding proteins stained intensely and distinctively on silver-stained sodium dodecyl sulfate-polyacrylamide gels and displayed an unusual sensitivity to reducing agents. The 32-kDa protein was not seen and did not bind 125I-labeled HeLa cell components if the EBs were solubilized in the presence of 2-mercaptoethanol. The 32-kDa protein was not affected by dithiothreitol, however. Similar to the effect of 2-mercaptoethanol, the 32-kDa protein was not visualized after treatment of EBs with the protease inhibitors tosyl-phenylalanine chloromethyl ketone (TPCK) or tosyl-lysine chloromethyl ketone (TLCK). TPCK and TLCK also abolished infectivity as did the alkylating agents N-ethylmaleimide and iodoacetamide, yet the latter two agents did not affect the appearance of the 32-kDa protein. These proteins were not detected in immunoblots with either rabbit antisera to C. trachomatis L2 EBs or by serum from a patient with lymphogranuloma venereum. The role of these proteins in the interaction of chlamydiae with host cells is not clear, but the binding of eucaryotic cell surface components and heparin, presence only during the infectious stage of the life cycle, variation between serotypes in correlation with disease, and sensitivity to reducing agents or protease inhibitors, collectively, suggest a role for these proteins in parasite-host interactions.

UI	MeSH Term	Description	Entries
D007457	Iodine Radioisotopes	Unstable isotopes of iodine that decay or disintegrate emitting radiation. I atoms with atomic weights 117-139, except I 127, are radioactive iodine isotopes.	Radioisotopes, Iodine
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D011480	Protease Inhibitors	Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).	Antiprotease,Endopeptidase Inhibitor,Endopeptidase Inhibitors,Peptidase Inhibitor,Peptidase Inhibitors,Peptide Hydrolase Inhibitor,Peptide Hydrolase Inhibitors,Peptide Peptidohydrolase Inhibitor,Peptide Peptidohydrolase Inhibitors,Protease Antagonist,Protease Antagonists,Antiproteases,Protease Inhibitor,Antagonist, Protease,Antagonists, Protease,Hydrolase Inhibitor, Peptide,Hydrolase Inhibitors, Peptide,Inhibitor, Endopeptidase,Inhibitor, Peptidase,Inhibitor, Peptide Hydrolase,Inhibitor, Peptide Peptidohydrolase,Inhibitor, Protease,Inhibitors, Endopeptidase,Inhibitors, Peptidase,Inhibitors, Peptide Hydrolase,Inhibitors, Peptide Peptidohydrolase,Inhibitors, Protease,Peptidohydrolase Inhibitor, Peptide,Peptidohydrolase Inhibitors, Peptide
D002352	Carrier Proteins	Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes.	Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D002689	Chlamydia	A genus of the family CHLAMYDIACEAE whose species cause a variety of diseases in vertebrates including humans, mice, and swine. Chlamydia species are gram-negative and produce glycogen. The type species is CHLAMYDIA TRACHOMATIS.
D003545	Cysteine	A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.	Cysteine Hydrochloride,Half-Cystine,L-Cysteine,Zinc Cysteinate,Half Cystine,L Cysteine
D006358	Hot Temperature	Presence of warmth or heat or a temperature notably higher than an accustomed norm.	Heat,Hot Temperatures,Temperature, Hot,Temperatures, Hot
D006367	HeLa Cells	The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for, among other things, VIRUS CULTIVATION and PRECLINICAL DRUG EVALUATION assays.	Cell, HeLa,Cells, HeLa,HeLa Cell
D006493	Heparin	A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts.	Heparinic Acid,alpha-Heparin,Heparin Sodium,Liquaemin,Sodium Heparin,Unfractionated Heparin,Heparin, Sodium,Heparin, Unfractionated,alpha Heparin
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man