FN Thomson Reuters Web of Science™ VR 1.0 PT J AU Goodwin, K Viboud, C Simonsen, L AF Goodwin, K Viboud, C Simonsen, L TI Antibody response to influenza vaccination in the elderly: A quantitative review SO VACCINE LA English DT Review DE influenza vaccine; antibodies; aging/immunology; review ID NURSING-HOME RESIDENTS; T-CELL RESPONSES; IMMUNE-RESPONSE; VIRUS VACCINE; SPLIT VACCINE; DOUBLE-BLIND; IMMUNOGENICITY; IMMUNIZATION; AGE; SERUM AB We performed a quantitative review of 31 vaccine antibody response studies conducted from 1986 to 2002 and compared antibody responses to influenza vaccine in groups of elderly versus younger adults. We did a weighted analysis of the probability of vaccine response (measured as seroconversion and seroprotection) for each vaccine component (H1, H3 and B antigens). Using a multiple regression model, we adjusted for factors that might affect the vaccine response. The adjusted odds-ratio (OR) of responses in elderly versus young adults ranged from 0.24 to 0.59 in terms of seroconversion and seroprotection to all three antigens. The CDC estimates of 70-90% clinical vaccine efficacy in young adults and these estimates suggest a corresponding clinical efficacy in the elderly of 17-53% depending on circulating viruses. We conclude that the antibody response in the elderly is considerably lower than in younger adults. This highlights the need for more immunogenic vaccine formulations for the elderly. (c) 2005 Elsevier Ltd. All rights reserved. C1 NIAID, Off Global Affairs, Bethesda, MD 20818 USA. NIH, Fogarty Int Ctr, Bethesda, MD 20892 USA. RP Simonsen, L (reprint author), NIAID, Off Global Affairs, 6610 Rockledge Dr,Room 2033, Bethesda, MD 20818 USA. EM lsimonsen@niaid.nih.gov OI Simonsen, Lone/0000-0003-1535-8526 NR 54 TC 431 Z9 447 U1 3 U2 24 PU ELSEVIER SCI LTD PI OXFORD PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND SN 0264-410X J9 VACCINE JI Vaccine PD FEB 20 PY 2006 VL 24 IS 8 BP 1159 EP 1169 DI 10.1016/j.vaccine.2005.08.105 PG 11 WC Immunology; Medicine, Research & Experimental SC Immunology; Research & Experimental Medicine GA 016VD UT WOS:000235647900014 PM 16213065 ER PT J AU Skiadopoulos, MH Biacchesi, S Buchholz, UJ Amaro-Carambot, E Surman, SR Collins, PL Murphy, BR AF Skiadopoulos, MH Biacchesi, S Buchholz, UJ Amaro-Carambot, E Surman, SR Collins, PL Murphy, BR TI Individual contributions of the human metapneumovirus F, G, and SH surface glycoproteins to the induction of neutralizing antibodies and protective immunity SO VIROLOGY LA English DT Article DE human metapneumovirus; neutralizing antibodies; protective immunity; glycoprotein ID RESPIRATORY SYNCYTIAL VIRUS; RECOMBINANT VACCINIA VIRUSES; AFRICAN-GREEN MONKEYS; SENDAI-VIRUS; G-PROTEIN; HEMAGGLUTININ-NEURAMINIDASE; MUCOSAL IMMUNIZATION; HOST IMMUNITY; IN-VITRO; TYPE-3 AB We evaluated the individual contributions of the three Surface glycoproteins of human metapneumovirus (HMPV), namely the fusion F, attachment G, and small hydrophobic SH proteins, to the induction of serum HMPV-binding antibodies, serum HMPV-neutralizing antibodies, and protective immunity. Using reverse genetics, each HMPV protein was expressed individually from an added gene in recombinant human parainfluenza virus type 1 (rHPIV 1) and used to infect hamsters once or twice by the intranasal route. The F protein was highly immunogenic and protective, whereas G and SH were only weakly or negligibly immunogenic and protective,. respectively. Thus, in contrast to other paramyxoviruses, the HMPV attachment G protein is not a major neutralization or protective antigen. Also, although the SH protein of HMPV is a virion protein that is Much larger than its counterparts in previously Studied paramyxoviruses, it does not appear to be a significant neutralization or protective antigen. Published by Elsevier Inc. C1 NIAID, Resp Viruses Sect, Infect Dis Lab, NIH,DHHS, Bethesda, MD 20892 USA. RP Skiadopoulos, MH (reprint author), NIAID, Resp Viruses Sect, Infect Dis Lab, NIH,DHHS, Bldg 50,Room 6511,50 S Dr MSC 8007, Bethesda, MD 20892 USA. EM mskiadopoulos@niaid.nih.gov RI Biacchesi, Stephane/A-6924-2010 FU Intramural NIH HHS NR 35 TC 66 Z9 72 U1 0 U2 0 PU ACADEMIC PRESS INC ELSEVIER SCIENCE PI SAN DIEGO PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA SN 0042-6822 J9 VIROLOGY JI Virology PD FEB 20 PY 2006 VL 345 IS 2 BP 492 EP 501 DI 10.1016/j.virol.2005.10.016 PG 10 WC Virology SC Virology GA 014GT UT WOS:000235468300018 PM 16300813 ER PT J AU Hortin, GL Shen, RF Martin, BM Remaley, AT AF Hortin, GL Shen, RF Martin, BM Remaley, AT TI Diverse range of small peptides associated with high-density lipoprotein SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS LA English DT Article DE high-density lipoprotein; apolipoprotein; peptidomics; transthyretin; apolipoprotein A-1; proteomics ID APOLIPOPROTEIN-A-I; OVARIAN-CANCER; PLASMA; IDENTIFICATION; DISEASE; PARAOXONASE; CAROTENOIDS; DISCOVERY; PROTEINS; URINE AB High-density lipoproteins (HDL) were examined as potential carriers of small peptides in plasma. HDL purified by density gradient centrifugation was delipidated and fractionated by size-exclusion chromatography Under denaturing conditions. By HPLC and mass spectrometry, more than 100 peptide components were found in the size range from 1000 to 5000 Da. By sequence analysis, peptides were identified as fragments of proteins Such as apolipoproteins, fibrinogen, alpha(1)-proteinase inhibitor, and transthyretin. The results indicate that purified HDL bears a complex range of small peptides. It is unclear whether the peptides have any significant functional role as apolipopeptides, but they may represent a pathway for peptide delivery or scavenging and a significant reservoir of plasma peptides for diagnostic evaluation. Published by Elsevier Inc. C1 NIH, Dept Lab Med, Bethesda, MD 20892 USA. NHLBI, NIH, Bethesda, MD 20892 USA. NIMH, NIH, Bethesda, MD 20892 USA. RP Hortin, GL (reprint author), NIH, Dept Lab Med, Bldg 10,Room 2C-407, Bethesda, MD 20892 USA. EM ghortin@mail.cc.nih.gov FU CLC NIH HHS [Z01 CL010342-03]; Intramural NIH HHS NR 26 TC 32 Z9 33 U1 1 U2 5 PU ACADEMIC PRESS INC ELSEVIER SCIENCE PI SAN DIEGO PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA SN 0006-291X J9 BIOCHEM BIOPH RES CO JI Biochem. Biophys. Res. Commun. PD FEB 17 PY 2006 VL 340 IS 3 BP 909 EP 915 DI 10.1016/j.bbrc.2005.12.098 PG 7 WC Biochemistry & Molecular Biology; Biophysics SC Biochemistry & Molecular Biology; Biophysics GA 009DR UT WOS:000235092000025 PM 16386709 ER PT J AU Bai, YW AF Bai, YW TI Energy barriers, cooperativity, and hidden intermediates in the folding of small proteins SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS LA English DT Article DE kinetic barrier; energy landscape; folding intermediates; cooperative stabilization; transition state ID NONNATIVE HYDROPHOBIC INTERACTIONS; STATE HYDROGEN-EXCHANGE; RD-APOCYTOCHROME B(562); SINGLE-DOMAIN PROTEINS; RATE-LIMITING STEP; TRANSITION-STATE; CHYMOTRYPSIN INHIBITOR-2; ENTHALPIC BARRIERS; KINETICS; DESOLVATION AB Current theoretical views of the folding process of small proteins (