<?xml version="1.0" encoding="UTF-8"?><rss version="2.0"
	xmlns:content="http://purl.org/rss/1.0/modules/content/"
	xmlns:wfw="http://wellformedweb.org/CommentAPI/"
	xmlns:dc="http://purl.org/dc/elements/1.1/"
	xmlns:atom="http://www.w3.org/2005/Atom"
	xmlns:sy="http://purl.org/rss/1.0/modules/syndication/"
	xmlns:slash="http://purl.org/rss/1.0/modules/slash/"
	>

<channel>
	<title>beta lactamases Archives - Online Biology Notes</title>
	<atom:link href="https://www.onlinebiologynotes.com/tag/beta-lactamases/feed/" rel="self" type="application/rss+xml" />
	<link></link>
	<description>A Complete notes for Students</description>
	<lastBuildDate>Tue, 18 Dec 2018 17:52:30 +0000</lastBuildDate>
	<language>en-US</language>
	<sy:updatePeriod>
	hourly	</sy:updatePeriod>
	<sy:updateFrequency>
	1	</sy:updateFrequency>
	
	<item>
		<title>ESBL (Extended Spectrum beta-Lactamases) and types </title>
		<link>https://www.onlinebiologynotes.com/esbl-extended-spectrum-beta-lactamases-and-types/</link>
		
		<dc:creator><![CDATA[Gaurab Karki]]></dc:creator>
		<pubDate>Thu, 11 Oct 2018 12:23:40 +0000</pubDate>
				<category><![CDATA[Pharmaceutical Microbiology]]></category>
		<category><![CDATA[beta lactamases]]></category>
		<category><![CDATA[CTX-M type ESBL]]></category>
		<category><![CDATA[OXA type ESBL]]></category>
		<category><![CDATA[PER type ESBL]]></category>
		<category><![CDATA[SHV type ESBL]]></category>
		<category><![CDATA[TEM type ESBL]]></category>
		<category><![CDATA[types of beta lactamases]]></category>
		<guid isPermaLink="false">http://www.onlinebiologynotes.com/?p=1709</guid>

					<description><![CDATA[<p>ESBL (Extended Spectrum beta-Lactamases) and types Extended spectrum Beta-lactamase are enzymes belongs to molecular class ‘A’ or ‘D’ and functional group 2b e and 2d. <a class="mh-excerpt-more" href="https://www.onlinebiologynotes.com/esbl-extended-spectrum-beta-lactamases-and-types/" title="ESBL (Extended Spectrum beta-Lactamases) and types ">[...]</a></p>
<p>The post <a href="https://www.onlinebiologynotes.com/esbl-extended-spectrum-beta-lactamases-and-types/">ESBL (Extended Spectrum beta-Lactamases) and types </a> appeared first on <a href="https://www.onlinebiologynotes.com">Online Biology Notes</a>.</p>
]]></description>
										<content:encoded><![CDATA[<h1>ESBL (Extended Spectrum beta-Lactamases) and types</h1>
<ul>
<li>Extended spectrum Beta-lactamase are enzymes belongs to molecular class ‘A’ or ‘D’ and functional group 2b e and 2d. These enzymes hydrolyses penicillin, cephalosporin (1<sup>st</sup>, 2<sup>nd</sup> and 3<sup>rd</sup> generaion) including Aztreonam. However they are inactivated by clavulinic acid ad cephamycin (cephoxitine and cephotetan).</li>
</ul>
<h2>Types of ESBL</h2>
<h3>1. TEM type ESBL (Temoneira)</h3>
<ul>
<li>This type of ESBL is commonly produced by <em>coli</em> and <em>Klebsiella pneumonia</em>, but also has been noted in <em>Neisseria gonorrhoae</em> and <em>Hemophilus influenza</em>.</li>
<li>All TEM type ESBLs are derived from TEM-1 and TEM-2</li>
<li>TEM-1 can hydrolyze ampicillin with greater extent but has negligible activity against extended spectrum cephalosporins. It is inhibited by clavulinic acid</li>
<li>TEM-2 has same hydrolytic profile as TEM-1 but has different isoelectric point.</li>
<li>There are more than 140 TEM type ESBl. However most common type of TEM ESBL are TEM-10, TEM-12 and TEM-26</li>
<li>Amino acid substitution in active site of enzyme is responsible for ESBL, which results in allowing excess amount of Oxy-imino-β-lactams.</li>
</ul>
<h3>2. SHV type ESBL (sulfhydryl variable)</h3>
<ul>
<li>SHV type ESBL resembles 80% to type TEM</li>
<li>SHV type is usually produced by <em>Klebsiella pneumonia</em> and other enterobacteriaceae.</li>
<li>SHV type are produced as a result of amino acid substitution at position 238 and 240.</li>
<li>More than 80 different types of SHV have been identified. Most common SHV type are SHV-5 and SHV-12</li>
</ul>
<h3>3. CTX-M type ESBL (Cefotaximases)</h3>
<ul>
<li>CTX-M type ESBL shows more affinity towards cefotaxims than other Oxyimino-β-lactam antibiotics.</li>
<li>Most common type of CTX-M are CTX-M-2, CTX-M-3, CTX-M-14, CTX-M-15</li>
<li>They are usually produced by <em> coli</em> and <em>Salmonella</em> enterica serovar Typhimurium</li>
</ul>
<h3>4. OXA type ESBl (Oxacillinases)</h3>
<ul>
<li>OXA type ESBl are usually produced by <em>Pseudomonas aeroginosa </em>but have been detected in other gram negative bacteria also.</li>
<li>This OXA type ESBL belongs to class ‘D’ and functional class 2d.</li>
<li>It is characterized by hydrolysis rate for cloxacillin and oxacillin greater than 50% than for benzylpenicillin.</li>
<li>They show reduced inhibition to clavulinic acid</li>
<li>Most OXA type beta-lactamase do not hydrolyse the extended spectrum cephalosporin to significant degree and are not regarded as ESBLs. However OXA-10 hydrolyses cefotaxime, ceftriaxone and aztreonam.</li>
<li>Most common type OXA type ESBL are is OXA-11, OXA-14, OXA-16, OXA-17, OXA-19, OXA-28, OXA-31, OXA-32, OXA_35, OXA-45</li>
</ul>
<h3>5. PER type ESBL:</h3>
<ul>
<li>It share only about 25-27% homology with TEM and SHV type ESBL</li>
<li>PER-1 can effectively hydrolyse penicillins and cephalosporins and is susceptible to clavulinic acid</li>
<li>PER type ESBl is produced by <em>Pseudomonas aeroginosa, Salmonella</em> enterica serovar Typhimurium , <em>Acinetobacter, Vibrio cholera, Klebsiella pneumonia, Proteus mirabilis</em></li>
</ul>
<h3>6. Other ESBL types are:</h3>
<ul>
<li><strong>VEB</strong></li>
<li><strong>BES-1</strong></li>
<li><strong>VIM-1</strong></li>
<li><strong>GES</strong></li>
<li><strong>TLA</strong></li>
<li><strong>IBC</strong></li>
<li><strong>SFO</strong></li>
</ul>
<h2>ESBL (Extended Spectrum beta-Lactamases) and types</h2>
<p>The post <a href="https://www.onlinebiologynotes.com/esbl-extended-spectrum-beta-lactamases-and-types/">ESBL (Extended Spectrum beta-Lactamases) and types </a> appeared first on <a href="https://www.onlinebiologynotes.com">Online Biology Notes</a>.</p>
]]></content:encoded>
					
		
		
			</item>
	</channel>
</rss>
