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	<title>enolase hijacking &#8211; BIOENGINEER.ORG</title>
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	<title>enolase hijacking &#8211; BIOENGINEER.ORG</title>
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		<title>Phage Protein Hijacks Host Enolase to Block Immunity</title>
		<link>https://bioengineer.org/phage-protein-hijacks-host-enolase-to-block-immunity/</link>
		
		<dc:creator><![CDATA[Bioengineer]]></dc:creator>
		<pubDate>Tue, 11 Nov 2025 13:02:48 +0000</pubDate>
				<category><![CDATA[Biology]]></category>
		<category><![CDATA[anti-CRISPR]]></category>
		<category><![CDATA[anti-CRISPR proteins]]></category>
		<category><![CDATA[enolase hijacking]]></category>
		<category><![CDATA[host enzyme exploitation]]></category>
		<category><![CDATA[microbial immunity mechanisms]]></category>
		<category><![CDATA[molecular mechanism]]></category>
		<category><![CDATA[phage-bacteria interaction]]></category>
		<category><![CDATA[type III CRISPR]]></category>
		<category><![CDATA[type III-A CRISPR systems]]></category>
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					<description><![CDATA[In a groundbreaking discovery that reshapes our understanding of the arms race between bacteria and viruses, researchers have identified a novel anti-CRISPR protein that cleverly exploits a host enzyme to subvert bacterial immune defenses. This newly characterized protein, AcrIIIA2, encoded by phages infecting the bacterium Streptococcus thermophilus, unveils an intricate mechanism by which viruses counteract [&#8230;]]]></description>
		
		
		
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