Tracer Study on AIMST University Students Using Data Mining

Tracer study is an approach which widely being used in most of the organization especially in the education institutions to track and to keep record of their students once they have graduated from the institution. Through tracer study, an institution able to evaluate the quality of education given to their graduates by knowing the graduates placements and positions in the society which later can be used as a benchmark in producing more qualified and competitive graduates. This tracer study basically focuses at one of the leading private university in the northern region of Peninsular Malaysia which known as AIMST University. This tracer study uses SPSS software as one the primary method to produce a relevant model of all the students’ enrolment as well as graduating students’ based on the data supplied by the Students and Records Division of AIMST University. However, the data supplied by the Student Admission and Records of AIMST University do contains missing values hence the data sets have to undergo cleaning process. As such CRISP methodology being applied to the datasets to ensure the data transformed into quality and usable data sets, with that the data will undergo pre processing approach. These data sets will be used in Data Mining approach in the modeling techniques to analyze the data and to identify the patterns

Two color morphs of the pelagic yellow-bellied sea snake, pelamis platura, from different locations of Costa Rica: snake venomics, toxicity, and neutralization by antivenom

artículo (preprint) -- Universidad de Costa Rica, Instituto de Investigaciones Clodomiro Picado, 2014The yellow-bellied sea snake, Pelamis platura, is the most broadly distributed snake species. Despite being endowed with a highly lethal venom, a proteomic analysis of its toxin composition was unavailable. The venoms of specimens collected in Golfo de Papagayo and Golfo Dulce (Costa Rica), where two distinctive color morphs occur, were chromatographically compared. The latter inhabits a fjord-like gulf where the transit of oceanic sea snakes into and from the basin is restricted, thus possibly affecting gene flow. RP-HPLC evidenced a conserved venom protein profile in both populations, despite their divergent color phenotypes. Following a trend observed in other sea snakes, P. platura venom is relatively simple, being composed of proteins of the three-finger toxin (3FTx), phospholipase A2 (PLA2), cysteine-rich secretory protein (CRISP), 5′-nucleotidase, and metalloproteinase families. The first three groups represent 49.9%, 32.9%, and 9.1% of total venom protein, respectively. The most abundant component (~ 26%) is pelamitoxin (P62388), a short-chain 3FTx, followed by a major basic PLA2 (~ 20%) and a group of three isoforms of CRISPs (~ 9%). Whereas isolated pelamitoxin was highly lethal to mice, neither the PLA2 nor the CRISP fraction caused death. However, the PLA2 rapidly increased plasma creatine kinase activity after intramuscular injection, indicating its myotoxic action. Differing from myotoxic PLA2s of viperids, this PLA2 was not cytolytic to murine myogenic cells in vitro, suggesting possible differences in its mechanism of action. The median lethal dose (LD50) estimates for P. platura crude venom in mice and in three species of fishes did not differ significantly. The sea snake antivenom manufactured by CSL Ltd. (Australia), which uses Enhydrina schistosa as immunogen, cross-recognized the three major components of P. platura venom and, accordingly, neutralized the lethal activity of crude venom and pelamitoxin, therefore being of potential usefulness in the treatment of envenomations by this species.Funded by grants from Ministerio de Economía y Competitividad, Madrid, BFU2010-17373; PROMETEO/2010/005 from the Generalitat Valenciana, Spain; Vicerrectoría de Investigación, Universidad de Costa Rica (741-B2-652 and 741-B3-760; Network for proteomic characterization of snake venoms of medical and biological relevance in Latin America), and CYTED (project BioTox, P211RT0412).UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP

Optimization of multimeric human papillomavirus L2 vaccines.

We sought to define the protective epitopes within the amino terminus of human papillomavirus (HPV) type 16 minor capsid protein L2. Passive transfer of mice with rabbit antisera to HPV16 L2 peptides 17-36, 32-51 and 65-81 provided significant protection against vaginal HPV16 challenge, whereas antisera to 47-66, 108-120 or 373-392 did not. Vaccination with L1 virus-like particles induces a high titer, but generally type-restricted neutralizing antibody response. Conversely, vaccination with L2 11-88, especially multimers thereof, induces antibodies that neutralize a broad range of papillomavirus types, albeit at lower titers than for L1 VLP. With the intent of enhancing the immunogenicity and the breadth of protection by focusing the immune response to the key protective epitopes, we designed L2 fusion proteins consisting of residues ∼11-88 of eight divergent mucosal HPV types 6, 16, 18, 31, 39, 51, 56, 73 (11-88×8) or residues ∼13-47 of fifteen HPV types (13-47×15). The 11-88×8 was significantly more immunogenic than 13-47×15 in Balb/c mice regardless of the adjuvant used, suggesting the value of including the 65-81 protective epitope in the vaccine. Since the L2 47-66 peptide antiserum failed to elicit significant protection, we generated an 11-88×8 construct deleted for this region in each subunit (11-88×8Δ). Mice were vaccinated with 11-88×8 and 11-88×8Δ to determine if deletion of this non-protective epitope enhanced the neutralizing antibody response. However, 11-88×8Δ was significantly less immunogenic than 11-88×8, and even the addition of a known T helper epitope, PADRE, to the construct (11-88×8ΔPADRE) failed to recover the immunogenicity of 11-88×8 in C57BL/6 mice, suggesting that while L2 47-66 is not a critical protective or T helper epitope, it nevertheless contributes to the immunogenicity of the L2 11-88×8 multimer vaccine

Site-specific PEGylation of native disulfide bonds in therapeutic proteins

Native disulfide bonds in therapeutic proteins are crucial for tertiary structure and biological activity and are therefore considered unsuitable for chemical modification. We show that native disulfides in human interferon alpha-2b and in a fragment of an antibody to CD4(+) can be modified by site-specific bisalkylation of the two cysteine sulfur atoms to form a three-carbon PEGylated bridge. The yield of PEGylated protein is high, and tertiary structure and biological activity are retained.Peer reviewe

Vaginal Challenge of Balb/c and C57BL/6 mice vaccinated with 11–88×8, 11–88×8Δ and 11–88×8ΔPADRE (11–88×8ΔP) in Alum+MPL.

<p>Balb/c or C57BL/6 mice were vaccinated three times at 2 week intervals with the indicated 11–88×8, 11–88×8Δ and 11–88×8ΔPADRE using Alum+MPL as adjuvant. The mice were vaginally challenged one month later using HPV16 pseudovirions carrying a luciferase reporter. Infection is measured as bioluminescence.</p

Peptide blockade of 11–88×8 antiserum.

<p>A. Sera of Balb/c mice immunized three times with 11–88×8 or 11–88×8Δ using Alum+MPL as adjuvant were harvested two weeks after the final boost. The antisera diluted 1∶100 were reacted with microtiter plates coated with 1 µg of two HPV16 L2 peptides encompassing residues 43–62 and 48–67. After washing, specific reactivity was measured by ELISA using peroxidase-linked anti-mouse IgG. B. Pooled sera of Balb/c mice immunized three times with 11–88×8 using Alum+MPL as adjuvant were harvested either pre-immunization (Pre-bleed) or two weeks after the final boost (×8 Sera). The antiserum to 11–88×8 was diluted 1∶50 in a total volume of 200 µl and incubated with 7 µg of HPV16 L2 peptide encompassing residues 13–32, 18–37, 23–42, 28–47, 33–52, 38–57, 43–62, 48–67, 53–72, 58–77, 63–82 or 71–90 for an hour prior to mixing with HPV16 pseudovirions carrying a SEAP reporter for a further hour at ambient temperature and subsequent infection of 293TT cells. Infection was measured as optical density, and only HPV16 L2 pepitdes 13–32 and 18–37 substantially blocked neutralization by 1∶3200 dilution of antiserum to 11–88×8. C. Sera of Balb/c mice immunized three times with 11–88×8 using Alum+MPL as adjuvant were harvested two weeks after the final boost and pooled (×8). The 11–88×8 antiserum was mixed with two HPV16 L2 peptides encompassing residues 43–62 and 48–67 (+Peptide) in the same ratios as in B. The 11–88×8 antiserum was administered i.p. either alone or pre-mixed with peptide in volumes of 20 µl, 5 µl or 2 µl to naïve mice (in groups of 5). Separate groups of mice received 200 µg each of antibody affinity purified with protein G columns from the sera of rabbits hyper-immunized with HPV16 L2 peptides 17–36, 47–66 or 373–392. All groups of mice (except the Background group) were subsequently challenged intra-vaginally with HPV16 pseudovirions carrying a luciferase reporter. Infection was assessed by measuring bioluminescence three days later.</p

Passive transfer of HPV16 L2 peptide antisera protects mice against vaginal challenge with HPV16.

<p>Mice were injected i.p. with 0.1 ml buffer or rabbit antiserum to KLH-coupled HPV16 L2 peptides encompassing residues 17–36, residues 32–51, residues 47–66, residues 65–81, 108–120, residues 373–392, or antiserum to HPV16 L1 VLP. One day later the mice were challenged intra-vaginally with HPV16 pseudovirion encoding luciferase.</p

HPV in vitro neutralization titers of sera of mice vaccinated with 13–47×15 and 11–88×8 in different adjuvants.

<p>Balb/c mice were vaccinated three times at 2 week intervals with the indicated 13–47×15 and 11–88×8 proteins formulated in alum, alum+MPL, alum+CpG or GPI-0100. Sera were harvested two weeks later for testing in vitro neutralization titers against HPV16 (A), HPV18 (B), HPV45 (C) and HPV58 (D) pseudovirions, or HPV16 at 3 months after the final vaccination (E).</p