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provides coniferyl ferulate(CAS#:161016-51-9) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Persistent, high-risk human papillomavirus (HPV) infection is the primary cause of cervical cancer. Neutralizing antibodies elicited by L1-only virus-like particles (VLPs) can block HPV infection; however, the lack of high-resolution structures has limited our understanding of the mode of virus infection and the requirement for type specificity at the molecular level. Here, we describe two antibodies, A12A3 and 28F10, that specifically bind to and neutralize HPV58 and HPV59, respectively, through two distinct binding stoichiometries. We show that the epitopes of A12A3 are clustered in the DE loops of two adjacent HPV58 L1 monomers, whereas 28F10 recognizes the HPV59 FG loop of a single monomer. Via structure-based mutagenesis and analysis of antibody binding, we further identified the residues HPV58 D154, S168, and N170 and HPV59 M267, Q270, E273, Y276, K278, and R283, which play critical roles in virus infection. By substituting these strategic epitope residues into other HPV genotypes, we could then redirect the type-specific binding of the antibodies to these genotypes, thus highlighting the importance of these specific residues, HPV58 R161, S168, and N308 and HPV59 Q270, E273, and D281. Overall, our findings provide molecular insights into potential structural determinants of HPV required for infectivity and type specificity.
human papillomavirus, infectivity, neutralization, structure, type specificity
Crystal Structures of Two Immune Complexes Identify Determinants for Viral Infectivity and Type-Specific Neutralization of Human Papillomavirus
Zhihai Li,a Daning Wang,b Ying Gu,a,b Shuo Song,a Maozhou He,b Jingjie Shi,a Xinlin Liu,a Shuangping Wei,a Jinjin Li,b Hai Yu,b Qingbing Zheng,b Xiaodong Yan,b,c Timothy S. Baker,c Jun Zhang,b Jason S. McLellan,corresponding authord Shaowei Li,corresponding authora,b and Ningshao Xiacorresponding authora,b
International Tuberculosis Campaign and Directorate-General of Health Services, New Delhi. Monthly Reports of BCG Statistics for July, August and September 1951 Including Supplements, Corrections and Progressive Totals
The bithorax complex (BX-C) of Drosophila, one of two complexes that act as master regulators of the body plan of the fly, is included within a sequence of 338,234 bp (SEQ89E). This paper presents the strategy used in sequencing SEQ89E and an analysis of its open reading frames. The BX-C sequence (BXCALL) contains 314,895 bp obtained by deletion of putative genes that are located at each end of SEQ89E and appear to be functionally unrelated to the BX-C. Only 1.4% of BXCALL codes for the three homeodomain-containing proteins of the complex. Principal findings include a putative ABD-A protein (ABD-AII) larger than a previously known ABD-A protein and a putative glucose transporter-like gene (1521 bp) located at or near the bithoraxoid (bxd), infra-abdominal-2 (iab-2) boundary on the opposite strand relative to that of the homeobox-containing genes.
Complete sequence of the bithorax complex of Drosophila.
C H Martin, C A Mayeda, C A Davis, C L Ericsson, J D Knafels, D R Mathog, S E Celniker, E B Lewis, and M J Palazzolo
1995 Aug 29