{"id":120755,"date":"2016-10-07T23:24:56","date_gmt":"2016-10-07T23:24:56","guid":{"rendered":"http:\/\/healthmedicinet.com\/i\/virginia-tech-scientists-solve-structure-of-enzyme-that-deactivates-important-antibiotic\/"},"modified":"2016-10-07T23:24:56","modified_gmt":"2016-10-07T23:24:56","slug":"virginia-tech-scientists-solve-structure-of-enzyme-that-deactivates-important-antibiotic","status":"publish","type":"post","link":"http:\/\/healthmedicinet.com\/i\/virginia-tech-scientists-solve-structure-of-enzyme-that-deactivates-important-antibiotic\/","title":{"rendered":"Virginia Tech scientists solve structure of enzyme that deactivates important antibiotic"},"content":{"rendered":"<p>A popular antibiotic called rifampicin, used to treat tuberculosis, leprosy, and Legionnaire&#8217;s disease, is becoming less effective as the bacteria that cause the diseases develop more resistance.<\/p>\n<p>One of the mechanisms leading to rifampicin&#8217;s resistance is the action of the enzyme Rifampicin monooxygenase.<\/p>\n<p>Pablo Sobrado, a professor of biochemistry in the College of Agriculture and Life Sciences, and his team used a special technique called X-ray crystallography to describe the structure of this enzyme. They also reported the biochemical studies that allow them to determine the mechanisms by which the enzyme deactivates this important antibiotic.<\/p>\n<p>The results were published in the <em>Journal of Biological Chemistry<\/em> and <em>PLOS One<\/em>, respectively.<\/p>\n<p>&#8220;In collaboration with Professor Jack Tanner at the University of Missouri and his postdoc, Dr. Li-Kai Liu, we have solved the structure of the enzyme bound to the antibiotic,&#8221; said Sobrado, who is affiliated with the Fralin Life Science Institute and the Virginia Tech Center for Drug Discovery. &#8220;The work by Heba, a visiting graduate student from Egypt, has provided detailed information about the mechanism of action and about the family of enzymes that this enzyme belongs to. This is all-important for drug design.&#8221;<\/p>\n<p>Heba Adbelwahab, of Damietta, Egypt, a graduate student in Sobrado&#8217;s lab, was a key player in the research and first author of the PLOS One paper.<\/p>\n<p>&#8220;Antibiotic resistance is one of the major problems in modern medicine,&#8221; said Adbelwahab. &#8220;Our studies have shown how this enzyme deactivates rifampicin. We now have a blueprint to inhibit this enzyme and prevent antibiotic resistance.&#8221;<\/p>\n<p>Rifampicin, also known as Rifampin, has been used to treat bacterial infections for more than 40 years. It works by preventing the bacteria from making RNA, a step necessary for growth.<\/p>\n<p>The enzyme, Rifampicin monooxygenase, is a flavoenzyme &#8212; a family of enzymes that catalyze chemical reactions that are essential for microbial survival. These latest findings represent the first detailed biochemical characterization of a flavoenzyme involved in antibiotic resistance, according to the authors.<\/p>\n<p>Tuberculosis, leprosy, and Legionnaire&#8217;s disease are infections caused by different species of bacteria. While treatable, the diseases pose a threat to children, the elderly, people in developing countries without access to adequate health care, and people with compromised immune systems.<\/p>\n<p>Virginia Tech<\/p>\n","protected":false},"excerpt":{"rendered":"<p>A popular antibiotic called rifampicin, used to treat tuberculosis, leprosy, and Legionnaire&#8217;s disease, is becoming less effective as the bacteria that cause the diseases develop more resistance. One of the mechanisms leading to rifampicin&#8217;s resistance is the action of the enzyme Rifampicin monooxygenase. Pablo Sobrado, a professor of biochemistry in the College of Agriculture and <a class=\"read-more-link\" href=\"http:\/\/healthmedicinet.com\/i\/virginia-tech-scientists-solve-structure-of-enzyme-that-deactivates-important-antibiotic\/\">Read More<\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[],"tags":[],"class_list":["post-120755","post","type-post","status-publish","format-standard","hentry"],"_links":{"self":[{"href":"http:\/\/healthmedicinet.com\/i\/wp-json\/wp\/v2\/posts\/120755","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/healthmedicinet.com\/i\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"http:\/\/healthmedicinet.com\/i\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"http:\/\/healthmedicinet.com\/i\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"http:\/\/healthmedicinet.com\/i\/wp-json\/wp\/v2\/comments?post=120755"}],"version-history":[{"count":0,"href":"http:\/\/healthmedicinet.com\/i\/wp-json\/wp\/v2\/posts\/120755\/revisions"}],"wp:attachment":[{"href":"http:\/\/healthmedicinet.com\/i\/wp-json\/wp\/v2\/media?parent=120755"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"http:\/\/healthmedicinet.com\/i\/wp-json\/wp\/v2\/categories?post=120755"},{"taxonomy":"post_tag","embeddable":true,"href":"http:\/\/healthmedicinet.com\/i\/wp-json\/wp\/v2\/tags?post=120755"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}