Tenecteplase, sold under the trade names TNKase, Metalyse and Elaxim, is an enzyme used as a thrombolytic drug. Tenecteplase is a tissue plasminogen activator (tPA) produced by recombinant DNA technology using an established mammalian cell line (Chinese hamster ovary cells). Tenecteplase is a 527 amino acid glycoprotein developed by introducing the following modifications to the complementary DNA (cDNA) for natural human tPA: a substitution of threonine 103 with asparagine, and a substitution of asparagine 117 with glutamine, both within the kringle 1 domain, and a tetra-alanine substitution at amino acids 296–299 in the protease domain. Tenecteplase is a recombinant fibrin-specific plasminogen activator that is derived from native t-PA by modifications at three sites of the protein structure. It binds to the fibrin component of the thrombus (blood clot) and selectively converts thrombus-bound plasminogen to plasmin, which degrades the fibrin matrix of the thrombus. Tenecteplase has a higher fibrin specificity and greater resistance to inactivation by its endogenous inhibitor (PAI-1) compared to native  t-PA. The abbreviation TNK is common for referring to tenecteplase, but abbreviating drug names is not best practice in medicine, and in fact "TNK" is one of the examples given on the Institute for Safe Medication Practices (ISMP) do-not-use list. Research
Researchers at Newcastle University in Australia say they have had a significant breakthrough in treating stroke patients using the commonly used drug. The findings were published in the New England Medical Journal.
Transmission via the secretions of carriers can result from direct interpersonal contact or contact with a contaminated surface. Bacteria on contaminated surfaces can be easily cultured. In conditions with sufficient nutrients, pneumococci can survive for 24 hours and avoid desiccation for multiple days. Reduced transmission has been observed amongst children with Pneumococcal conjugate vaccine (PCV) immunization as acquisition of a new strain of S. pneumoniae is inhibited by pre-existing colonization. Immunoglobulin G (IgG) immunization with high antibody concentration can also inhibit acquisition. These antibodies require the agglutinating function of the Fc fragment. For successful acquisition in a new host, pneumococcus must successfully adhere to the mucous membrane of the new host’s nasopharynx. Pneumococcus is able to evade detection by the mucous membrane when there is a higher proportion of negatively charged capsules. This clearance is mediated by Immunoglobulin A1 (IgA1) which is abundant on the URT mucosal surfaces. Colonization
Transparent and opaque colony morphology has been observed for pneumococci. Airway colonization is observed in transparent phenotypes of serotypes, while survival in bloodstreams is observed for opaque phenotypes. Colonizable strains exhibit resistance against neutrophilic immune response. Successful colonization requires S. pnuemoniae to evade detection by the nasal mucus and attach to epithelial surface receptors. Asymptomatic colonization occurs when S. pneumoniae bind to N-acetyl-glucosamine on epithelium without inflammation. However, co-infection with a pre-existing inflammatory URT infection results in an over-expression of the epithelial receptors utilized by S. pneumoniae, thus increasing the likelihood of colonization.