Successful seroconversion against diphtheria and tetanus induced through maternal vaccination in a region of Colombia

Doracelly Hincapie-Palacio,Adriana Echeverri,Cristina Hoyos,Felipe Vargas-Restrepo,Marta Ospina,Seti Buitrago,Jesús Ochoa 대한백신학회 2022 Clinical and Experimental Vaccine Research Vol.11 No.1

Purpose: This study aims to compare protection against diphtheria and tetanus conferred on the mother and the neonate before and after maternal vaccination against tetanus, diphtheria, and acellular pertussis (Tdap), transfer of antibodies, and the variables that could impact on the protection. Materials and Methods: The study followed a cohort of 200 pregnant women from a region in Colombia, contacted during prenatal control before vaccination and upon delivery. The work determined immunoglobulin G antibodies against diphtheria and tetanus of pregnant women and umbilical cord. The proportion of protection, the geometric mean of the concentration, and the transfer of maternal antibodies were calculated. The protection profile of the pregnant women was explored by using multiple correspondence analysis. Results: The concentration of antibodies against diphtheria was significant before and after vaccination of the pregnant women (p=0.000) with proportions of 85.0% and 97.5%, respectively, and of 98.6% in the umbilical cord, with significant antibody correlation (Spearman’s coefficient=0.668, p=0.01). Sero-protection against tetanus before vaccination was at 71.0%, after at 92.6%, and in the umbilical cord at 95.9%, with significant antibody concentration before and after vaccination (p=0.000) and antibody correlation (Spearman’s coefficient=0.936, p=0.01). Sero-protection was higher when the pregnant women were vaccine 8 to 11 weeks before delivery. Unprotected pregnant women were those not vaccinated during pregnancy. Conclusion: The high proportion of protection against diphtheria and tetanus and the placental transfer support the need to promote maternal immunization with Tdap

A Proteomics Platform Combining Depletion, Multi-lectin Affinity Chromatography (M-LAC), and Isoelectric Focusing to Study the Breast Cancer Proteome

Zeng, Zhi,Hincapie, Marina,Pitteri, Sharon J.,Hanash, Samir,Schalkwijk, Joost,Hogan, Jason M.,Wang, Hong,Hancock, William S. American Chemical Society 2011 ANALYTICAL CHEMISTRY - Vol.83 No.12

<P>The discovery of breast cancer associated plasma/serum biomarkers is important for early diagnosis, disease mechanism elucidation, and determination of treatment strategy for the disease. In this study of serum samples, a multidimensional fractionation platform combined with mass spectrometric analysis were used to achieve the identification of medium to lower abundance proteins, as well as to simultaneously detect glycan and abundance changes. Immuno-affinity depletion and multi-lectin chromatography (M-LAC) were integrated into an automated HPLC platform to remove high abundance protein and fractionate glycoproteins. The collected glycoproteomes were then subjected to isoelectric focusing (IEF) separation by a digital ProteomeChip (dPC), followed by in-gel digestion and LC–MS analysis using an Orbitrap mass spectrometer. As a result, the total number of identified proteins increased significantly when the IEF fractionation step was included as part of the platform. Relevant proteins with biological and disease significance were observed and the dynamic range of the serum proteome measurement was extended. In addition, potential glycan changes were indicated by comparing proteins in control and cancer samples in terms of their affinity to the multi-lectin column (M-LAC) and the p<I>I</I> profiles in IEF separation. In conclusion, a proteomics platform including high abundance protein depletion, lectin affinity fractionation, IEF separation, and LC–MS analysis has been applied to discover breast cancer-associated proteins. The following candidates, thrombospondin-1 and 5, alpha-1B-glycoprotein, serum amyloid P-component, and tenascin-X, were selected as promising examples of the use of this platform. They show potential abundance and glycan changes and will be further investigated in future studies.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/ancham/2011/ancham.2011.83.issue-12/ac2002802/production/images/medium/ac-2011-002802_0006.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/ac2002802'>ACS Electronic Supporting Info</A></P>

Lectin-mediated microfluidic capture and release of leukemic lymphocytes from whole blood

Vickers, Dwayne A. L.,Hincapie, Marina,Hancock, William S.,Murthy, Shashi K. Springer-Verlag 2011 Biomedical microdevices Vol.13 No.3

The Use of Plasma Glycoproteomics for the Early Detection of Disease

W.S. Hancock,M. Hincapie,M. Kullolli,T. Plavina 한국당과학회 2008 한국당과학회 학술대회 Vol.2008 No.1

Mechanisms underlying disease pathogenesis are not well understood in the context of common etiological factors such as microbial infection, inflammation, malignancy or tissue breakdown. Such processes may be elucidated by identifying disease-related molecular markers, such as acute phase proteins, cytokines, cytoskeletal fragments and autoantigens. In an attempt to identify such markers, we have developed a novel platform, namely multiple lectin affinity chromatography (M-LAC) to study the plasma glycoproteome in patients and healthy donors in a series of studies ranging from cancer to autoimmune disease. The M-LAC platform allowed the evaluation of changes in concentration of glycoproteins, and to comprehensively survey the plasma proteome. We then used a second method, intact peptidomics, to assess changes in endogenous proteolytic activity by analyzing the low molecular weight (LMW) component of blood. The integrated proteomic and peptidomic analysis of plasma samples identified a number of cytoskeletal and Ca2+-binding proteins and their proteolytic fragments in the disease samples. The measurements were compared to healthy donors and several of the observed differential quantitations were independently verified by ELISA. The identified changes in plasma proteome and peptidome, and the underlying changes in glycosylation together with altered endogenous protease activity may result in the generation of novel autoantigens. We and others have confirmed this hypothesis by the observation of autoantibodies in patients and upon extension of these studies to larger populations of patient; we may gain additional understanding of the role of etiological factors in different disease pathways.

Economic burden and treatment patterns of gynecologic cancers in the United States: evidence from the Medical Expenditure Panel Survey 2007–2014

Xiaomeng Yue,Jane M. Pruemer,Ana L. Hincapie,Ziyad S. Almalki,Jeff J. Guo 대한부인종양학회 2020 Journal of Gynecologic Oncology Vol.31 No.4

Objective: This study estimated nationally representative medical expenditures ofgynecologic cancers, described treatment patterns and assessed key risk factors associatedwith the economic burden in the United States. Methods: A retrospective repeated measures design was used to estimate the effect ofgynecologic cancers on medical expenditures and utilization among women. Data wereextracted from the Medical Expenditure Panel Survey (weighted sample of 609,787 US adults)from 2007 to 2014. Using the behavioral model of health services utilization, characteristicsof cancer patients were examined and compared among uterine, cervical, and ovarian cancerpatients. Multivariable linear regression models were conducted on medical expenditure witha prior logarithmic transformation. Results: The estimated annual medical expenditure attributed to gynecologic cancers was$3.8 billion, with an average cost of $6,293 per patient. The highest annual cost per personwas ovarian cancer ($13,566), followed by uterine cancer ($6,852), and cervical cancer($2,312). The major components of medical costs were hospital inpatient stays (53%, $2.03billion), followed by office-based visits (15%, $559 million), and outpatient visits (13%, $487million). Two key prescription expenditures were antineoplastic hormones (10.3%) andanalgesics (9.2%). High expenditures were significantly associated with being a marriedwoman (p<0.001), having private health insurance (p<0.001), being from a low- and middle income family (p<0.001), or living in the Midwest or the South (p<0.001). Conclusion: The key risk factors and components were well described for the economicburden of gynecologic cancers. With a growing population of cancer patients, efforts toreduce the burden of gynecologic cancers are warranted.

A Chromosome-centric Human Proteome Project (C-HPP) to Characterize the Sets of Proteins Encoded in Chromosome 17

Liu, Suli,Im, Hogune,Bairoch, Amos,Cristofanilli, Massimo,Chen, Rui,Deutsch, Eric W.,Dalton, Stephen,Fenyo, David,Fanayan, Susan,Gates, Chris,Gaudet, Pascale,Hincapie, Marina,Hanash, Samir,Kim, Hoguen American Chemical Society 2013 JOURNAL OF PROTEOME RESEARCH Vol.12 No.1

<P>We report progress assembling the parts list for chromosome 17 and illustrate the various processes that we have developed to integrate available data from diverse genomic and proteomic knowledge bases. As primary resources, we have used GPMDB, neXtProt, PeptideAtlas, Human Protein Atlas (HPA), and GeneCards. All sites share the common resource of Ensembl for the genome modeling information. We have defined the chromosome 17 parts list with the following information: 1169 protein-coding genes, the numbers of proteins confidently identified by various experimental approaches as documented in GPMDB, neXtProt, PeptideAtlas, and HPA, examples of typical data sets obtained by RNASeq and proteomic studies of epithelial derived tumor cell lines (disease proteome) and a normal proteome (peripheral mononuclear cells), reported evidence of post-translational modifications, and examples of alternative splice variants (ASVs). We have constructed a list of the 59 “missing” proteins as well as 201 proteins that have inconclusive mass spectrometric (MS) identifications. In this report we have defined a process to establish a baseline for the incorporation of new evidence on protein identification and characterization as well as related information from transcriptome analyses. This initial list of “missing” proteins that will guide the selection of appropriate samples for discovery studies as well as antibody reagents. Also we have illustrated the significant diversity of protein variants (including post-translational modifications, PTMs) using regions on chromosome 17 that contain important oncogenes. We emphasize the need for mandated deposition of proteomics data in public databases, the further development of improved PTM, ASV, and single nucleotide variant (SNV) databases, and the construction of Web sites that can integrate and regularly update such information. In addition, we describe the distribution of both clustered and scattered sets of protein families on the chromosome. Since chromosome 17 is rich in cancer-associated genes, we have focused the clustering of cancer-associated genes in such genomic regions and have used the ERBB2 amplicon as an example of the value of a proteogenomic approach in which one integrates transcriptomic with proteomic information and captures evidence of coexpression through coordinated regulation.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jprobs/2013/jprobs.2013.12.issue-1/pr300985j/production/images/medium/pr-2012-00985j_0009.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/pr300985j'>ACS Electronic Supporting Info</A></P>