| pubmed-article:8926104 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8926104 | lifeskim:mentions | umls-concept:C0032064 | lld:lifeskim |
| pubmed-article:8926104 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:8926104 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
| pubmed-article:8926104 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8926104 | lifeskim:mentions | umls-concept:C0020965 | lld:lifeskim |
| pubmed-article:8926104 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:8926104 | pubmed:dateCreated | 1996-11-14 | lld:pubmed |
| pubmed-article:8926104 | pubmed:abstractText | The structural gene for V antigen (lcrV) is known to be encoded within the lcrGVH-yopBD operon of the approximately 70-kb low-calcium-response or Lcr plasmid of Yersinia pestis. This 37-kDa monomeric peptide was reported to provide active immunity in mice, suppress inflammatory cytokines, and regulate expression of the low calcium response (Lcr+). Here we describe pVHB62, encoding a polyhistidine-V antigen fusion peptide (Vh) and linked LcrH. Vh underwent degradation from both the C terminus and N terminus during classical chromatographic fractionation but remained intact within two compartments during Ni2+ affinity chromatography. The first was homogeneous, capable of active immunization (mouse intravenous 50% lethal dose, > 10(7) bacteria), and stable at 4 degrees C. The second remained bound to the affinity column but could be eluted as a mixture of Vh, LcrH, and low-molecular-weight material by application of 6 M guanidine HCl. This mixture was dialyzed, denatured in 8 M urea, and again applied to the affinity column, which then hound Vh but not LcrH. The latter was recovered and renatured, and low-molecular-weight material was removed by biochemical fractionation. The resulting homogeneous LcrH bound protein AN antigen fusion peptide but not protein A in a sandwich enzyme-linked immunosorbent assay, and this reaction was inhibited by Vh. These observations indicate that LcrH normally binds V antigen in bacterial cytoplasm and suggest that only free LcrH down-regulates expression of the low calcium response. | lld:pubmed |
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| pubmed-article:8926104 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8926104 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8926104 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8926104 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8926104 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8926104 | pubmed:issn | 0019-9567 | lld:pubmed |
| pubmed-article:8926104 | pubmed:author | pubmed-author:BrubakerR RRR | lld:pubmed |
| pubmed-article:8926104 | pubmed:author | pubmed-author:MotinV LVL | lld:pubmed |
| pubmed-article:8926104 | pubmed:author | pubmed-author:NedialkovY... | lld:pubmed |
| pubmed-article:8926104 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8926104 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:8926104 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8926104 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8926104 | pubmed:pagination | 4313-8 | lld:pubmed |
| pubmed-article:8926104 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8926104 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8926104 | pubmed:articleTitle | V antigen-polyhistidine fusion peptide: binding to LcrH and active immunity against plague. | lld:pubmed |
| pubmed-article:8926104 | pubmed:affiliation | Department of Microbiology, Michigan State University, East Lansing 48824-1101, USA. | lld:pubmed |
| pubmed-article:8926104 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8926104 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:8926104 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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