A comprehensive review of the nasal microbiome in chronic rhinosinusitis (CRS).

Chronic rhinosinusitis (CRS) has been known as a disease with strong infectious and inflammatory components for decades. The recent advancement in methods identifying microbes has helped implicate the airway microbiome in inflammatory respiratory diseases such as asthma and COPD. Such studies support a role of resident microbes in both health and disease of host tissue, especially in the case of inflammatory mucosal diseases. Identifying interactive events between microbes and elements of the immune system can help us to uncover the pathogenic mechanisms underlying CRS. Here we provide a review of the findings on the complex upper respiratory microbiome in CRS in comparison with healthy controls. Furthermore, we have reviewed the defects and alterations of the host immune system that interact with microbes and could be associated with dysbiosis in CRS.

Pharmacist advice to asthmatics regarding antihistamine use.

Due to the frequency of asthmatics having concurrent allergic symptoms, patients may seek relief from antihistamines, which are currently labeled with warnings against their use in asthmatics. A survey was conducted in the Chicago area to evaluate the advice rendered by pharmacists regarding the use of antihistamines in asthmatics and their opinions about the current product labeling. Thirty percent of the surveys were returned. Nearly half (48%) of the surveyed pharmacists advise their asthmatic customers to avoid antihistamines and 75% of this group recommend avoidance because they believe antihistamines worsen asthmatic symptoms, despite the lack of sufficient clinical data to support this concern. Only 17% of pharmacists advise that antihistamines pose no problems for asthmatics. The latter group is the most aware that there is controversy surrounding the current labeling. Overall, half the pharmacists surveyed believe the current labeling is not appropriate for patients with asthma. Until the labeling is revised, physicians should be aware that pharmacists may advise their asthmatics against using antihistamines even though antihistamines should be only contraindicated in cases of proven adverse reactions.

Anaphylaxis following ingestion of a psyllium-containing cereal.

Recently, psyllium hydrophilic mucilloid, a bulk-forming laxative, has been added to breakfast cereals for cholesterol-lowering effects. We report a case of a 60-year-old woman with no prior history of psyllium ingestion who developed anaphylactic symptoms after eating a psyllium-containing cereal. Her only previous exposure was dispensing a psyllium-containing laxative as a nurse. Immunoglobulin E-mediated sensitization was documented by skin testing and basophil histamine release. The literature is reviewed regarding allergic reactions to psyllium. Health care workers and pharmaceutical workers handling psyllium may be at increased risk due to sensitization from inhalation. Physicians and consumers should be aware of potential serious reactions from eating psyllium-containing cereals even without prior history of ingestion of psyllium.

Lack of cross-reactivity between IgE to salmon and protamine sulfate.

Immediate type-generalized reactions to protamine sulfate are uncommon but may be fatal. The mechanisms of severe or fatal reactions are unknown in most cases. One theory is that contaminating fish (salmon) proteins present in protamine solutions induce anaphylaxis in salmon-sensitive subjects. A second hypothesis is that protamine interacts with anti-salmon IgE to cause anaphylaxis. We assessed these hypotheses by establishing an indirect amplified enzyme-linked immunosorbent assay (ELISA) for IgE to salmon. Sera obtained from two subjects anaphylactically sensitive to salmon demonstrated high binding to salmon that was not inhibited by preincubation of sera with 500 or 1000 micrograms of protamine or Aspergillus fumigatus. Serum from a patient who experienced anaphylactic shock from protamine was indistinguishable from control sera in the ELISA for IgE to salmon. Anti-protamine IgE could not be demonstrated in separate experiments. The assays prove that 1) serum IgE to salmon is not inhibited by protamine and 2) serum from a patient experiencing a severe reaction to protamine did not contain IgE to salmon or protamine. The experiments do not support the notion that there is cross-reactivity between IgE to salmon and protamine sulfate in the cases evaluated.

Potentiation of human basophil histamine release by protamine: a new role for a polycation recognition site.

Protamine is an arginine-rich basic polypeptide that stimulates histamine release from rat mast cells but not from human basophils. In this report, we show that protamine causes a non-cytolytic potentiation of IgE-mediated histamine release from human basophils. A direct effect of protamine on basophils was supported by results obtained using cell preparations containing 35-65% basophils. The potentiation occurred at all concentrations of antigen that initiated release and was most pronounced at antigen concentrations that alone stimulated minimal histamine release. The kinetics of potentiated release were parallel to those for IgE-mediated histamine release, and addition of protamine did not overcome the block caused by antigenic desensitization. Staging experiments indicated that enhancement occurred only when protamine and antigen were added together in a single step reaction. Protamine also potentiated release stimulated by eosinophil granule major basic protein or poly-L-lysine, but inhibited release initiated by poly-L-arginine; poly-L-arginine stimulated release was also inhibited by polymyxin B. Arginine-rich histone mimicked the protamine effect, while lysine-rich histone, polymyxin B, and compound 48/80 had minimal or no effect on IgE-mediated release. These results suggest that a polycation recognition site on human basophils similar to that described for rat mast cells may mediate potentiation of basophil secretory events by arginine-rich basic polypeptides.

Raman spectra of crystalline lysozyme, pepsin, and alpha chymotrypsin.

Satisfactory Raman spectra of crystalline lysozyme, pepsin, and alpha chymotrypsin were obtained with laser excitation. The spectra are very similar to each other, but show enough minor differences to make this a useful method of identification. The readily identified bands assignable to specific groupings are noted.