The difference of the mean from the peak value is due to the long tails of the distribution for large distances Tyrosine Kinase Inhibitor Library solubility dmso that are the effect of small gaps in the glycoprotein positions. The HA glycoproteins are 70 Å at their widest and are therefore well-separated on average and not in contact at their ectodomains. Based on our models of the HAs, we calculate the fractional volume occupied by the glycoproteins on the surface, defined here as a layer beyond the membrane one HA molecule thick. The fractional volume values for the three X-31 virions reported

in Fig. 3 are 13.5%, 15.0%, and 15.5% and for the three Udorn virions, 15.2%, 16.8%, and 19.2%. The fraction of the membrane surface area that the HA covers in projection is roughly twice the volume fraction value, and reflects the fact that the HA deviates from a cylinder in shape so that the head domain hides volume close to the membrane. Fig. 4a shows a model for the glycoprotein positions on one surface of an X-31 virion with a fractional volume of 13%. The surface is surprisingly open in contrast

check details to the impression from viewing the virus in projection images. Because the HA is recognized by neutralizing antibodies, we considered which parts of the protein are accessible to antibodies in the context of the virus surface. While the sequence variable head domain is likely to be exposed, one consequence of the open packing is that epitopes near the membrane

are accessible. Fig. 4c shows the previously described crystal structure [7] of the HA in complex with an Fab from the broadly neutralizing antibody FI6 that recognizes an epitope in the stem domain. In Fig. 4a, several HA positions are shown where there is enough room for 3 Fabs to bind a single HA without clashing into another HA position. Fig. 4b shows a Udorn surface of slightly higher fractional volume (15%). Several positions are also shown Thymidine kinase where there is enough room for an HA to bind a single Fab, and typically each glycoprotein can be oriented to bind at least one Fab. Though we have assessed the locations where Fabs can bind using a rigid Fab model, when the known flexibility of the Fab is considered, there are likely to be even fewer constraints on binding the stem region. A striking feature of the virus particles is the curvature of the membrane. For capsule or filament-shaped viruses of the most typical dimension in our preparations, the virus has a small radius of curvature perpendicular to the long axis of the capsule (Fig. 5). One consequence of this curvature would be a geometric constraint on the fraction of the virus surface that could engage with receptors on a target surface. The receptor binding site is located near the top of the HA as shown by the purple ligand in Fig. 4c. We calculate the relative distance of the receptor binding sites (Fig.

Manufacturing of recombinant proteins in plants for influenza vaccine development evolved as an alternative to the conventional egg-based vaccine production to overcome the limitations in quantity and time consumption [13]. This

bottleneck of egg-produced vaccines can have serious consequences during influenza Gemcitabine concentration pandemics, when the production of sufficient amounts of vaccine in an adequate time frame to serve the global market could be difficult. Regarding the need of rapidly produced vaccines in times of pandemics and the time consuming limitation of the egg-based vaccines, the here presented study tested the recombinant antigen of a highly immunogenic H1N1 strain responsible for the 2009/2010 pandemic. Furthermore, the study extends the

published work with HAC1 and SiO2 and evaluates the immunogenicity of this vaccine formulation when combined with c-di-GMP and administered at the site of virus entry. Overall, it showed the potential of the c-di-GMP/SiO2 double-adjuvanted vaccine to induce systemic humoral and strong mucosal immune responses, with IgA in the airways. Furthermore, it presented evidence of antigen-primed T-cells in the lung in intratracheally vaccinated mice. Female wild-type BALB/c mice Enzalutamide nmr aged 6–8 weeks (Charles River, Sulzfeld, Germany) were kept at an animal facility under conventional housing conditions (22 °C, 55% humidity, 12-h day/night cycle) with food and tap water ad libitum. The randomized study was approved by a local agency (Application-No. 33.9-42502-04-11/0465) and conducted according to the German Animal Protection law. Reagents were, if not stated otherwise, purchased from Sigma–Aldrich (Munich, Germany). Phosphate buffered saline (PBS) without Ca2+ and Mg2+, pH 7.4, Dulbecco’s Modified Eagle’s Medium/Nutrient

Mixture F-12 HAM (DMEM) with l-glutamine, 15 mM HEPES and 7.5% w/v sodium bicarbonate without phenol red, pH 7.2–7.4, Adenosine RPMI 1640 and Earle’s Balanced Salt Solution (EBSS) were obtained from Gibco (Darmstadt, Germany). Cell/tissue cultivation medium was supplemented with 100 U/mL penicillin and 100 μg/mL streptomycin. HAC1 was produced as previously described [14]. Briefly, the HA nucleotide sequence, encompassing amino acids 18–530 of the A/California/04/09 influenza strain (H1N1, NCBI accession number ACQ76318.1) were optimized for expression in plants and synthesized. The optimized HA sequence contains a 6× His affinity purification tag and the ER retention signal KDEL at the C-terminus. This gene was inserted into the pGRD4 launch vector and transformed into Agrobacterium tumefaciens. The transformed bacterium was introduced into hydroponically grown Nicotiana benthamiana by vacuum infiltration and leaf tissues were harvested, homogenized, extracted, filtered and chromatographically purified after a one-week growing period [14]. Aliquots of purified HAC1 were kept in PBS at −80 °C until usage.

Briefly, nitrocellulose bottom 96-well plates (MILLIPORE) were coated overnight at 4 °C with anti-IFN-γ monoclonal antibody (clone R4-6A2; www.selleckchem.com/products/dorsomorphin-2hcl.html BD Biosciences) diluted in PBS. Plates were washed and blocked for 2 h with DMEM supplemented with 10% FCS. Spleen

cells of immunized mice were prepared in DMEM supplemented with 10% FCS and recombinant IL-2 (100 U/ml). Splenocytes were seeded at a density of 5 × 105 cells/well and stimulated with F3 antigenic fraction (5 μg/ml) during 20 h at 37 °C, 5% CO2. Plates were washed and incubated for 4 h, at room temperature, with a biotin-conjugate anti-mouse IFN-γ monoclonal antibody (clone XMG1.2; BD Biosciences) and, after the next wash step, with peroxidase-labeled streptavidin, for 2 h at room temperature. Reactions were detected with a peroxidase substrate containing 3,3′-diaminobenzidine Tyrosine Kinase Inhibitor Library mw tetrahydrochloride (1 mg/ml) and 30% hydrogen peroxide solution (1 μl/ml) in 50 mM Tris–HCL buffer, pH = 7.5. Reactions were stopped under running water, and spots were counted on a S5 Core ELISPOT Analyser (CTL). Four weeks after the boost immunization, mice were infected orally with 20 cysts of P-Br strain of T. gondii, obtained from macerated brains of infected Swiss-Webster reservoirs suspended in PBS. Animals were sacrificed 8 weeks after the challenge. The brains were collected, macerated and suspended in 1 ml of PBS. Cysts were counted, in

duplicates, under light microscope, in 10 μl of brain suspensions. All results were evaluated for their statistic significance by Student’s t-test (parametric data) or by Mann–Whitney test (non-parametric data) performed with Minitab version 14. Normal distribution of samples was assessed by Anderson Darling software. The recombinant NA38-SAG2 segment was developed to carry the SAG2 sequence of T. gondii flanked by the duplicated 3′ promoter and the extended native 5′ terminal sequence of 70 nucleotides corresponding to 28 nt of the 5′ promoter and a duplication

of the those last 42 nt of the NA coding sequence, located upstream the promoter ( Fig. 1). Recombinant Influenza A viruses harboring the dicistronic NA38-SAG2 segment (FLU-SAG2) were generated using the 12 plasmid-driven reverse genetics, as previously described [41]. Recombinant FLU-SAG2 viruses displayed a slightly altered phenotype ( Fig. 2A), but showed infectious titers (9.2 ± 3.2 × 107 pfu/ml) similar to wild type vNA (1.4 × 108 pfu/ml). The presence of SAG2 in recombinant NA segments was assessed in three FLU-SAG2 clones by RT-PCR with primers that allowed the amplification of the entire region of insertion of SAG2. As shown in Fig. 2B, amplification products of the expected size (∼900 bp) were observed for all clones analyzed. Moreover, these amplicons were sequenced and showed no mutation in SAG2 sequence as well as in the internal 3′promoter (data not shown). Taking together, these results showed that FLU-SAG2 viruses are genetically stable in cell culture.

We also identified and investigated restaurants with more than two foodborne illness reports in the same year, since most restaurants appeared to have one or two reports, and because the CDC defines a foodborne disease outbreak as more than one case of a similar illness due to consumption of a common food (Daniels et al., 2002 and Jones et al., 2013). We extracted food

vehicles mentioned in the FOOD outbreak reports and the Yelp data according to the CDC convention of categorizing and grouping implicated Crenolanib nmr foods (Painter et al., 2009 and Painter et al., 2013). Broadly, the taxonomy consisted of three major categories: aquatic animals, land animals and plants. These categories were hierarchically distributed into subcategories as shown in Fig. 2. Initially, we grouped the data into five major categories: aquatic, dairy–eggs, fruits–nuts, meat–poultry, and vegetables. Based on observations from this grouping, we further analyzed nineteen more specific categories,

capturing all the major food groups. The nineteen categories consisted of fish, crustaceans, mollusks, dairy, eggs, beef, game, pork, poultry, grains–beans, fruits–nuts, fungi, leafy, root, sprout, vine-stalk, shellfish, vegetables, and meat. The aquatic, shellfish, vegetables and meat categories consisted of all foods that belonged Selleck GDC973 to these categories but could not be assigned to the more specific categories such as leafy, crustaceans, poultry, etc. We excluded the oils–sugars category since most meals include natural or processed oils and/or sugars. Foods implicated in foodborne illness were either categorized as simple or complex. Simple foods consisted of a single ingredient (e.g., lettuce) or could be classified into a single category

(e.g., fruit salad). Complex foods consisted of multiple ingredients that could be classified into more than one commodity (e.g., pizza). For example, if pizza were implicated in an alleged foodborne illness report, we documented three food categories: grains–beans (crust), vine-stalk (tomato sauce), and dairy (cheese). If a report included a food item not easily identifiable (such as a traditional dish), we used Google search GPX6 engine to locate the main ingredients in a typical recipe (e.g., meat, vegetable, aquatic, etc.) and categorized the food accordingly. To compare foods implicated by Yelp and the CDC, we focused on reports from 2006 to 2011, because the 2012 Yelp data were incomplete. We ranked the nineteen food categories separately for Yelp and FOOD, according to the frequency with which each food category was implicated per year. Food categories with the same frequency were assigned the average of their rankings. Correlations of the ranked food categories were assessed using Spearman’s rank correlation coefficient, ρ. Analyses were performed in SAS 9.1.3 (SAS Institute, Inc., Cary, NC). De-identified reviews of 13,262 businesses closest to 29 U.S. colleges in fifteen states (Table A.

At predetermined intervals of time, 3 ml of sample solution was withdrawn from receptor compartment to determine the permeation of FVS, and refilled with the equal volume of the fresh Phosphate Buffer pH 6.8. The samples were analyzed by RP-HPLC analytical method for drug content determination. Triplicate observations of each sample were measured. Cumulative amount of drug permeated through rat skin in μg/cm2 from different formulated patches were plotted against time (h). 8 Based on in-vitro permeation profile of FVS Flux (Jss, μg/cm2/h), Permeability coefficient (Kp,

cm/h), Diffusion coefficient (D, cm2/h) & Lag Time (TL, cm2/s) were determined. In-vitro permeation profile of optimized formulation was determined through human cadaver epidermis and Epigenetic inhibitor compared against the permeation profile through rat skin for the significant difference in release. Data obtained from the in-vitro release study Pictilisib supplier were fitted to different kinetic models (Zero order, First order, Higuchi’s model & Korsmeyer–Peppas model) to understand the release mechanism of prepared patches. Different kinetic

models used for matrix type transdermal patches were compared by their R2 values to understand best fitted model. FVS analysis was carried out using RP-HPLC technique by using gradient system HPLC (Cyberlab, USA) with a C18 column (BDS HYPERSIL®, 150 × 4.6 mm, 5 μm). The mobile phase was Idoxuridine prepared by methanol:phosphate buffer pH 3:acetonitrile at the ratio of 5:3:2 v/v. The pH of the mobile phase was adjusted to 3.0 with phosphoric acid (85%). Prepared mobile phase was filtered under

vacuum by using Millipore membrane (0.2 μm) and degassed using ultrasonicator. The mobile phase was pumped at a flow rate of 1.0 ml/min through the column at ambient temperature. 20 μl samples were introduced by injection in the HPLC system with 235 nm as a detection wavelength. Run time was kept at 10 min and retention time was 6.4 min.9 Skin irritation study was carried out by the draize patch test. The dorsal surface of the Wister albino rat (weight 400–500 g) was shaved carefully 24 h prior to the application of patch.10 Ethical clearance of the protocol was obtained from the Institutional Animal Ethical Committee of Noble Group of Institutions. Optimized (formulation F9) patch was adhered properly on the hairless dorsal surface of the rat for 4 h within the area of 3.14 cm2. The skin irritation was observed after predetermined time interval and extent of irritation (by edema and erythema) was ranked from 0 (no evidence of irritation) to 4 (severe irritation). Accelerated stability study was carried out according to ICH guideline for 6 months. The samples were analyzed for the flux at the interval of 0, 30, 60, 90 & 180 days and were compared with permeation profile of unconstrained patch.

While 30% of participants in the neutral orthoses group had some discomfort, only 1% was rated as severe. While prescription of insoles is inexpensive and simple, it is now clear that lateral insoles provide no therapeutic or disease modifying benefit and cause discomfort in a large percentage of patients. This study should sound the death knell for the use of lateral wedged insoles for the treatment of medial compartment knee osteoarthritis. “
“Neuromuscular deficits have been linked with chronic musculoskeletal conditions. The use of ultrasound imaging (USI)

to aid rehabilitation of neuromusculoskeletal disorders has been called rehabilitative ultrasound imaging (RUSI) I-BET151 supplier and defined as ‘a procedure used by physical therapists to evaluate muscle and related soft tissue morphology and function during exercise and physical tasks. RUSI is used to assist in the application of therapeutic interventions, providing feedback to the patient and physical therapist (Teyhen, 2006). Brightness mode (b-mode) USI is the most common form used by physical

therapists and will be the focus of this summary. Clinical utility: USI can distinguish between healthy adults XL184 molecular weight and those with low back pain (LBP). Those with LBP have decreased muscle thickness, side-to-side asymmetry, and decreased ability to thicken the muscles during a contraction ( Teyhen et al 2009). Moreover, when measured by USI, lumbar multifidus muscle asymmetry appears to be predictive of future episode of LBP up to three years later ( Hides et al 2001). Finally, USI can distinguish between changes in muscle thickness during common LBP exercises when performed by healthy adults ( Teyhen et al 2008) and is preliminarily supported as a biofeedback tool to enhance exercise effectiveness ( Henry and Teyhan 2007). Criterion-related validity: In a recent systematic review Koppenhaver et al (2009a) concluded that b-mode USI when applied in a unless rehabilitative setting is a valid tool to measure trunk muscle size and muscle activation

during most submaximal contracted states. When comparing muscle thickness obtained by magnetic resonance imaging and USI, researchers have demonstrated substantial agreement (ICC 0.84 to –0.95) with only minimal differences between the modalities (0.03 to 0.21 cm2) ( Hides et al 1995, 2006). Although comparisons between electromyography and change in muscle thickness obtained by USI have most often demonstrated a curvilinear relationship ( Hodges et al 2003), the ability of USI to measure muscle activation is likely context-dependent and is based on the muscle being measured, the task performed, and the intensity of the contraction ( Koppenhaver et al, 2009a). Responsiveness to change: Motor control training has been demonstrated to increase multifidus cross sectional area (p = 0.004), decrease side-to-side asymmetry, and was associated with a 50% reduction in pain ( Hides et al 2008b).

Although these questionnaires may be valuable, they are time consuming to administer. Therefore, modifications and abbreviations of the Tampa Scale for Kinesiophobia, Angiogenesis inhibitor Roland Morris Disability Questionnaire, and SF-36 have been developed and validated to make them easier to What is already known on this topic: The Tampa Scale for Kinesiophobia, Roland Morris Disability Questionnaire, EQ-5D, and 36-item Short Form are recommended outcome measures in people with sciatica. What this study adds: Asking people how much they fear that their

sciatica would be increased by physical activity predicts both perceived recovery and pain severity at one year. This single question explains more of the variation in pain severity than the Tampa Scale for Kinesiophobia. Individual questions about disability and general health were not consistently predictive of 1-year outcomes. This was an observational study using the data of 135 people with sciatica who participated in a randomised controlled trial that assessed the cost-effectiveness of physical therapy plus general practitioner care versus general practitioner care alone (Luijsterburg et al 2007). Of 170 people screened, 11% were ineligible and 9% refused to participate. Measures were taken at baseline, at 3, 6 and 12 weeks, and at 1 year. General practitioners in Rotterdam selleck screening library and the surrounding area invited people

with acute sciatica to participate. Participants were required to be aged 18 to 65 years, to be able to speak and read Dutch, and to have radiating Ergoloid pain in the leg

extending to below the knee with a duration of < 6 weeks and a severity of pain scored above 3 on an 11-point numerical rating scale (NRS) where 0 = no pain and 10 = maximum pain (Von Korff et al 2000). Another inclusion criterion was the presence of one of the following symptoms: more pain on coughing, sneezing or straining, decreased muscle strength in the leg, sensory deficits in the leg, decreased reflex activity in the leg or a positive straight leg raise test. The Tampa Scale for Kinesiophobia, Roland Morris Disability Questionnaire, EQ-5D and SF-36 were completed at baseline. In a consensus meeting of the investigators of the trial, newly devised questions that were thought to be able to cover and therefore substitute for the entire questionnaire (ie, substitute questions) were discussed and chosen on the basis of consensus. Each substitute question was answered on an 11-point numerical rating scale, as described below. The substitute questions were devised and used in Dutch but have been translated by a native speaker for publication in English. The substitute questions were completed at the same time as the questionnaires. Kinesiophobia: The Tampa Scale for Kinesiophobia is a validated questionnaire to measure fear of movement ( Haugen et al 2008, Kori et al 1990).

In addition, we observed Selleckchem Ibrutinib that incorporation of gD did not change the molar ratio of the NDV HN and F proteins relative to the nucleocapsid and matrix proteins, and did not appear to affect the yield of particles or their infectivity. These results suggest that space is not a constraint in the incorporation of foreign proteins into envelope of NDV. At the present, we do not know the basis for the highly efficient incorporation of the gD protein in the NDV virion. One possibility is

that some feature of the amino acid sequence of the transmembrane domain or cytoplasmic tail of the native BHV-1 gD makes it more efficient for inclusion in particles. Another possibility is that gD might accumulate at the cell surface in a higher molar amount compared to the NDV proteins, leading to more efficient incorporation. However, it remains unexplained why the chimeric gD protein containing the cytoplasmic and

transmembrane from the NDV F protein accumulated efficiently at the cell surface yet was not significantly incorporated. One potential consequence of incorporating such high amounts of gD into the virus particles was that it might lead to an increase in virulence of the NDV vector, but this was not observed for the MDT and ICPI tests in chickens. Furthermore, the rLaSota/gDFL virus remained as restricted for replication in selleck kinase inhibitor bovines as the LaSota empty vector and the rLaSota/gDF vaccine. In summary, for the first time we have evaluated the potential of an avian virus as a vaccine

vector for bovine use. The commonly used NDV vaccine strain LaSota was used to express the gD of BHV-1. Our results showed that calves vaccinated with the recombinant viruses elicited an immune response against the gD and provided partial protection from BHV-1 challenge. These results suggested that the gD could be a useful component of a mucosal vaccine against BHV-1 infection. These vectored vaccine candidates are highly attenuated for replication in cattle Ketanserin and are not shed into the environment. Furthermore, the observation that NDV has a negligible incidence of recombination with other circulating viruses in cattle population makes it a promising and safe vaccine delivery vector candidate for bovine population. This strategy may be useful for the development of live viral vectored vaccines against foreign animal diseases for which currently safe and effective vaccines are not available. We thank Daniel Rockemann and all our laboratory members for their excellent technical assistance and help. This research was supported in part by NIAID contract no. N01A060009 (85% support) and the NIAID, NIH Intramural Research Program (15% support). The views expressed herein do not necessarily reflect the official policies of the Department of Health and Human Services; nor does mention of trade names, commercial practices, or organizations imply endorsement by the U.S. Government. “
“The highest incidence of meningococcal disease is in infants <12 months of age [1].

Dengue virus, a mosquito-borne emerging or re-emerging pathogen belongs to the family flaviviridae. There are four distinct serotypes of dengue

(1–4) 1 that infect humans, causing diseases ranging from acute self-limiting febrile illness to life-threatening dengue hemorrhagic fever and Dengue Shock Syndrome. 2 and 3 In the past decade, more than 50–100 million human were infected 4, 5 and 6 causing 24,000 deaths every year, 7 neither vaccine nor antiviral learn more therapy is licensed for the prevention or treatment of dengue virus infections. 8 and 9 Other medically important flaviviruses, West Nile virus, yellow fever virus, Japanese encephalitis virus and tick-borne encephalitis virus also cause significant human mortality and morbidity. 10 Single-stranded flaviviral genome of dengue

virus is approximately 11 kb in length. The genome encodes three structural proteins Capsid (C), Pre-membrane (P), and Envelope (E), in addition to seven non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5). 11 NS5 is the largest and most highly conserved flaviviral protein, with greater than 75% sequence identity VE-821 chemical structure in dengue 1–4 serotypes. NS5 is particularly important for viral replication, it functions as an RNA-dependent RNA polymerase (RdRp) 12 and 13 and N-terminal domain contains S-Adenosyl-l-Methionine (SAM) dependent methyltransferase (MTase) activity. 14 MTase plays key roles in normal physiology and human infection through methylating DNA, RNA and proteins. 15, 16 and 17 The enzyme has two specific binding sites; the position of SAH indicates the binding site of the methyl donor, SAM. RNA cap analogs bind (-)-p-Bromotetramisole Oxalate to a shallow second pocket formed between sub domains 1 and 2 (Fig. 1). The two binding sites are connected by a common Y-shaped cleft which suggests the placement of capped RNA along the cleft positioning the first RNA nucleotide close to SAM compatible

with 2′-O-methylation.18 The binding site of SAM, SAH and RTP is conserved among Flavivirus MTases, but not among the host SAM-utilizing enzymes. The earlier studies indicated that the binding pockets are functionally important for both MTase function and viral replication. The inhibitors developed so far are not specific to the Flavivirus MTase, resulting in toxicity. Currently no clinically approved antiviral therapy is available for treatment of Flavivirus-associated diseases. 18, 19, 20, 21, 22, 23 and 24 So far, the computational techniques were employed for identification of the novel lead molecules to inhibit dengue virus MTase,19 in which the SAM binding site and RNA cap were considered for docking study using Auto dock software package. Further, cyclopentapeptide inhibitors were discovered for the both sites using high throughput virtual screening and structure-based ligand design methods.20 Moreover, 5 million commercially available compounds were screened against the two binding sites of this enzyme independently.

Recombinant protein-based vaccines must be further evaluated for antigen stability. The PfCP-2.9 efficacy correlated with the integrity of its tertiary structure maintained by inter-molecular disulfide bonds. Accumulated evidence has Decitabine solubility dmso indicated that reduced and alkylated components in PfCP-2.9 lost their GIA activities [4]. Therefore, assessing the conformational nature of this protein following the emulsion process was extremely important for vaccine development. To date, there were

no available methods for the detection of intact protein once it had been emulsified. The Montanide ISA720 adjuvant has been widely utilized in HIV and malaria vaccine development and it was shown to be an effective delivery system for human vaccines [13], [14], [15] and [16]. However, Montanide ISA720 has been reported to modify the antigen after emulsification [21]. Therefore, the stability of the formulated emulsion with the adjuvant was an initial concern. We used available methods as well as new developed methods (such as the sandwich ELISA method) to assess the stability and

potency of the PfCP-2.9 vaccine formulation. This ELISA-based Temsirolimus cost method utilized two types of antibodies and demonstrated that emulsified PfCP-2.9 maintained its integrity for periods of up to 18 months suggesting that protein integrity would not easily be lost in ISA720 adjuvant formulations stored at 4 °C. Furthermore, no degradation of PfCP-2.9 was observed by SDS-PAGE for samples stored for up to 2 years. We noted that PfCP-2.9 formed aggregates (which increased over time in samples stored at warmer temperatures) in some of the emulsion preparations but these aggregates were a small percentage of total protein. However, the aggregates retained their tertiary structure as noted by the ability of mAb5.2 else to bind to them in Western blot assays. Moreover, the potency of the stored emulsion containing aggregated PfCP-2.9 was not affected and the stored emulsion

induced specific antibodies that inhibited parasite growth at the same level as a freshly prepared antigen emulsions, indicating that aggregate formation did not influence the potency and function of the vaccine emulsion. Taken together, the physical and biological properties of the vaccine emulsion preparations used in the described pre-clinical studies demonstrated that PfCP-2.9 was stable for at least 1.5 years. Although some protein aggregation was observed during storage at 4 °C, the aggregated protein retained its conformational integrity and immunogenic potency. This investigation received financial support from the National Basic Research Program (973 Program) in China (2007CB513100) the National 863 Program (2006AA02A222), and Shanghai leading Academic Discipline Project (B901). “
“Bovine herpesvirus-1 (BHV-1) is a pathogen of major economic importance in the cattle industry worldwide.