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Aeryun Kim,Stephanie L. Servetas,Jieun Kang,Jinmoon Kim,장성일,Yun Hui Choi,Hanfu Su,Yeong-Eui Jeon,Youngmin A. Hong,유윤정,D. Scott Merrell,차정헌 한국미생물학회 2016 The journal of microbiology Vol.54 No.12
The array of outer membrane proteins (OMPs) found in Helicobacter pylori provides a crucial component for persistent colonization within the gastric niche. Not only does H. pylori harbor a wide number of OMPs, but these OMPs often vary across strains; this likely contributes to immune evasion, adaptation during long term colonization, and potentially differential disease progression. Previous work from our group described OMP differences among the Bab family (babA, babB, and babC) and Hom family (homA and homB) from 80 American H. pylori clinical isolates (AH) and 80 South Korean H. pylori clinical isolates (KH). In the current study, we expanded our investigation to include the less well characterized Hom family member, HomC. Overall, we identified and genotyped three homC variants: homCS, homCL, and homCM, in both populations. Similar to other polymorphic genes, the KH group showed less overall diversity, with 97.5% of strains harboring homCL. In contrast, a more heterogeneous profile was observed in strains derived from an American population; we found nearly equal distribution of homCS and homCL. Further analysis of the AH group identified associations between homC polymorphism and bab genotype; in AH strains, there was a significant association between homCL and carriage of babA at locus A. Since babA is an important virulence factor for the development of severe gastric disease, these data may suggest that homC polymorphism plays a role in H. pylori pathogenesis.
Wong, Sook-San,Yoon, Sun-Woo,Zanin, Mark,Song, Min-Suk,Oshansky, Christine,Zaraket, Hassan,Sonnberg, Stephanie,Rubrum, Adam,Seiler, Patrick,Ferguson, Angela,Krauss, Scott,Cardona, Carol,Webby, Richard Elsevier 2014 Virology Vol.468 No.-
<P><B>Abstract</B></P> <P>The cleavage motif in the hemagglutinin (HA) protein of highly pathogenic H5 and H7 subtypes of avian influenza viruses is characterized by a peptide insertion or a multibasic cleavage site (MBCS). Here, we isolated an H4N2 virus from quails (Quail/CA12) with two additional arginines in the HA cleavage site, PEK<B>RR</B>TR/G, forming an MBCS-like motif. Quail/CA12 is a reassortant virus with the HA and neuraminidase (NA) gene most similar to a duck-isolated H4N2 virus, PD/CA06 with a monobasic HA cleavage site. Quail/CA12 required exogenous trypsin for efficient growth in culture and caused no clinical illness in infected chickens. Quail/CA12 had high binding preference for α2,6-linked sialic acids and showed higher replication and transmission ability in chickens and quails than PD/CA06. Although the H4N2 virus remained low pathogenic, these data suggests that the acquisition of MBCS in the field is not restricted to H5 or H7 subtypes.</P> <P><B>Highlights</B></P> <P> <UL> <LI> An H4N2 influenza virus with a multibasic cleavage site in the hemagglutinin protein was isolated from quails. </LI> <LI> This virus remained lowly pathogenic in chickens and required trypsin for <I>in vitro</I> growth. </LI> <LI> This virus showed higher preference for mammalian-type sialic acid receptors. </LI> <LI> This virus transmitted better in chicken than a duck-origin H4N2 virus. </LI> </UL> </P>