Implementation of a Vascular Access Experience Program to Train Unit-Based Vascular Access Champions.

Vascular access team (VAT) nurses receive many consults to place short peripheral catheters (SPCs), a portion of which do not require skilled insertion by a VAT member. VAT nurses at a health care organization in the Midwestern United States developed a program to train direct care nurses as unit-based vascular access champions to increase and improve SPC placement, care, and maintenance. Twenty-one nurses from 6 units were selected to train as vascular access champions; knowledge and confidence around SPC placement were assessed before, immediately after, and 6 months after the training.

Specific IgE antibody responses to ragweed allergens Ra5S and Ra5G associated with distinct HLA-DR beta genes.

Previous studies have established that sensitivity (IgE antibody response) to Ra5S, a 5000 mol. wt protein of short ragweed pollen, is significantly associated with host possession of HLA-DR2. The same allele was implicated [Goodfriend et al.

Allergen nomenclature.

This article presents a nomenclature system for allergens which has been officially recommended by the International Union of Immunological Societies (IUIS). The nomenclature is based on proposals of the IUIS Sub-Committee for Allergen Nomenclature and is applicable to highly purified, well-characterized allergens and to non-purified or partially purified allergenic extracts.

Ra5G, a homologue of Ra5 in giant ragweed pollen: isolation, HLA-DR-associated activity and amino acid sequence.

Recent studies [Marsh et al. (1982) J. exp.

500-MHz 1H NMR studies of ragweed allergen Ra5.

The solution conformation of short ragweed allergen Ra5, a protein of 45 amino acid residues cross-linked with four disulfide bridges, has been investigated by 1H NMR spectroscopy at 500 MHz. The aromatic region, which contains resonances from three tyrosines and two tryptophans, has been partially assigned. Two tyrosines titrate with a pK of 10.

Immunochemical and genetic studies of Amb.t. V (Ra5G), an Ra5 homologue from giant ragweed pollen.

Giant ragweed pollen allergen Amb.t. V (Ra5G), a homologue of short ragweed pollen Amb.

Unusual emission properties of the tryptophans at the surface of short ragweed allergen Ra5.

The fluorescence and low-temperature phosphorescence of short ragweed pollen allergen Ra5 have been examined. Both the fluorescence of Ra5 in aqueous solution at room temperature and the phosphorescence of Ra5 in rigid glycol-water solvents at low temperature result entirely from the tryptophan residues in the molecule. The heterogeneity in the low-temperature phosphorescence spectra indicates that the two tryptophans in Ra5 are located in distinct environments and can be studied independently.

Two variants of ragweed allergen Ra3.

Two disc electrophoretic forms of Ra3 (I and II) were isolated by column chromatography in yields of 30 and 10 mg/kg pollen, respectively. On the basis of 8% carbohydrate content (determined for Ra3I and assumed for Ra3II), the major and minor forms had essentially identical molecular weights (12,300 daltons). Although their amino acid compositions were similar, a number of single residue differences were found, some of which were confirmed in separate studies on the complete amino acid sequences of Ra3I and Ra3II.

Amino acid sequence of ragweed allergen Ra3.

The complete amino acid sequence of ragweed pollen allergen Ra3 has been determined. The molecule consists of 101 amino acid residues and to date is the only allergen isolated from Ambrosia elatior (short ragweed) which contains carbohydrate. This particular preparation of allergen has a single, unique amino acid sequence, but there is evidence suggesting that, like Ra5, Ra3 isolated from pollen collected in diverse geographical areas shows amino acid sequence variation.

Skin reactivity to purified pollen allergens in highly ragweed-sensitive individuals.

Five hundred twenty-five atopic patients were skin tested over a 12-mo period to several crude allergens with a puncture skin-testing technique utilizing a bifurcated needle originally developed for smallpox immunization. Of these, 122 were highly allergic to short ragweed pollen and were subsequently tested with a series of purified grass and ragweed allergens. Data of their reactivity to these allergens is presented, and the phenomenon that each patient has a unique "allergic fingerprint" to purified pollen allergens is shown.

Reactivity of ragweed allergens with IgE antibodies. Analyses by leukocyte histamine release and the radioallergosorbent test and determination of cross-reactivity.

Five distinct proteins with allergenic activity have been isolated from short ragweed pollen. We initially tested three of these, AgE, AgK, and Ra3, for reactivity with IgE antibodies by leukocyte histamine release and by the radioallergosorbent test (RAST). We found highly significant correlations between the reactivities of these allergens by leukocyte histamine release and by the RAST, consistent with the view that both procedures detected comparable allergenic activity.

HLA-B7 cross-reacting group and human IgE-mediated sensitivity to ragweed allergen Ra5.

HLA typing and cutaneous testing for allergen sensitivity of 76 ragweed allergic patients confirmed previous findings of a significant association between sensitivity to ragweed allergen Ra5 and possession of one or other of the HLA-B7 cross-reacting group of antigens.

'Mapping' of postulated Ir genes within HLA by studies in allergic populations.

Analysis of specific IgE responses to highly purified allergens provides a particularly good model to study the genetics of human immune response. The use of this model is illustrated by studies of large populations of allergic individuals in terms of their HLA phenotype, basal total IgE level and specific IgE-mediated sensitivities to rye grass group I (Rye I) and to ragweed Ra3. We find significant associations between HLA-B8 and Rye I response and HLA-A2 and Ra3 response, which become more striking in those atypical allergic subjects who have low total IgE levels.

The amino acid sequence of ragweed pollen allergen Ra5.

The complete amino acid sequence of Ra5, a ragweed pollen allergen, has been determined. Allergen Ra5 is a low molecular weight protein of 45 residues derived from Ambrosia elatior, the short ragweed. It contains no detectable carbohydrate or lipid and has four disulfide bridges.

Chemistry of a low molecular weight ragweed pollen allergen RA5, and association of human responsiveness to RA5 with HL-A7 cross-reacting group.

A protein allergen, Ra5, was isolated by column chromatographic procedures from the aqueous extract of short ragweed pollen by Lapkoff and Goodfriend. The allergen was obtained in a highly homogenous form, was devoid of carbohydrate and had the low molecular weight of 5100 daltons. A report will be given of studies by Marsh, Bias, Hsu and Goodfriend on the cutaneous activity of Ra5 in 105 antigen E-sensitive patients along with HL-A typing of these patients.

Association of the HL-A7 cross-reacting group with a specific reaginic antibody response in allergic man.

A relatively small proportion (17 percent) of individuals highly allergic to ragweed were found to develop marked reaginic (immunoglobulin E-mediated) skin sensitivity to a minor ragweed pollen allergen Ra5 (molecular weight 5200). Sensitivity to Ra5 was significantly associated with the possession of a major histocompatibility antigen of the HL-A7 cross-reacting group. This appears to be the first evidence of a strong association between a specific immune response and a specific group of closely related HL-A antigens in man.