Effect of ampicillin and chloroquine on humoral immune response elicited by bovine albumin encapsulated in liposomes

Abstract

Several studies have been conducted to establish the phenomenon of vaccine-drug interaction against various categories of chemotherapeutic agents, such as fluoroquinolones and chloramphenicol (1). They can either increase or decrease the phagocytic function or modulate the immune response triggered by an antigen (2). Investigations have revealed that chloroquine prophylaxis for malaria is associated with an impaired antibody response to rabies vaccine administered intradermally (3). It was proposed that chloroquine might interfere with the antigen processing mechanism and T-cell recognition (4, 5). In addition, chloroquine raises pH within lysosomes and thus interferes with the fusion of viral and lysosomal membranes, which is necessary to release viral nucleocapsid. It has been also shown that chloroquine interferes with secretion of interleukin-1 (IL-1) by monocytes, inhibiting the generation of immunoglobulin secretary lymphocytes (4). However, chloroquine did not affect the antibody response of yellow fever vac- Immune suppression resulting from chemoprophylaxis and potential drug interaction were investigated in experimental animals pre-medicated with ampicillin and chloroquine followed by immunization with bovine serum albumin bearing liposomes prepared by the reverse phase evaporation method. The prepared liposomes were evaluated for particle size, entrapment efficiency and in vitro release. Humoral immune response was measured in terms of systemic IgG antibody titre by the ELISA method. The present study showed that 7:3 molar ratio of soya phosphatidylcholine and cholesterol produced liposomes of mean diameter of 235.4 ± 10.3 nm and entrapment efficiency of 41.3 ± 3.2%. Ampicillin significantly (p < 0.05) decreased the antibody titre whereas chloroquine did not reduce the antibody titre significantly. The study will help in programming a new drug management and in characterization of vaccine-drug interaction.

Preparation of Casein Biopeptide-Loaded Niosomes by High Shear Homogenization and Their Characterization

“…It was observed that 99% of peptides in their free form were released within 6 h, while peptides from niosomes showed the burst release to the extent of 41% during the first hour of dialysis under simulated GI conditions (pH of 1.2) because of the fast diffusion of peptide molecules located on the surface, followed by controlled release under simulated intestinal conditions (pH 7.4). This kind of protein release profile has also been observed for BSA-loaded niosomal vesicles. , The initial burst release was presumably due to the presence of peptides in the free form in the niosomes, while the sustained release to the extent of 85.54% by 24 h was probably due to their encapsulation into niosomal bilayers. Raslan showed that the profile of ketoprofen release from niosomes occurred in two distinct phases; an initial phase in which rapid drug leakage was observed in the first 6 h to the extent of 50–60%, followed by slow release of only 20% in the next 6 h. Moreover, proteins such as insulin encapsulated in niosomal vesicles showed a similar sustained release .…”

“…This kind of protein release profile has also been observed for BSA-loaded niosomal vesicles. 28,51 The initial burst release was presumably due to the presence of peptides in the free form in the niosomes, while the sustained release to the extent of 85.54% by 24 h was probably due to their encapsulation into niosomal bilayers. Raslan 52 showed that the profile of ketoprofen release from niosomes occurred in two distinct phases; an initial phase in which rapid drug leakage was observed in the first 6 h to the extent of 50−60%, followed by slow release of only 20% in the next 6 h. Moreover, proteins such as insulin encapsulated in niosomal vesicles showed a similar sustained release.…”

Formulation and Characterization of Bovine Serum Albumin-Loaded Niosome

“…1) (31). Briefly, set amounts of Span 60 (Table I) with different percentages of CH (0%, 20%, 40%, 60%, and 80%) (Table II) were dissolved in 5 ml of diethyl ether.…”

Scientific Opinion on Chloramphenicol in food and feed

“…Few experimental studies have been published on immune disturbance of chloramphenicol, and these studies did not follow the systematic immunotoxicity protocols as is currently customary for immunotoxicity risk assessment, including quantitative aspects (WHO, 2012). Madan et al (2007) studied antibody production in male albino rats (8-12 weeks of age) after s.c. bovine serum albumin (BSA) immunisation, following treatment with ciprofloxacin (i.m. administration of 0.33 mg/kg b.w.…”