Management of non-parasitic splenic cysts: does size really matter?

BACKGROUND: Splenic cysts are relatively rare clinical entities and are often diagnosed incidentally upon imaging conducted for a variety of clinical complaints. They can be categorized as primary or secondary based on the presence or absence of an epithelial lining. Primary cysts are further subdivided into those that are and are not secondary to parasitic infection. The treatment of non-parasitic splenic cysts (NPSC) has historically been dictated by two primary factors: the presence of symptoms attributable to the cyst and cyst size greater or less than 5 cm. While it is appropriate to resect a symptomatic lesion, the premise of recommending operative intervention based on size is not firmly supported by the literature. METHODS: In the current study, we identified 115 patients with splenic cysts and retrospectively reviewed their management that included aspiration, resection, or observation. RESULTS: Our data reveal a negative overall growth rate of asymptomatic cysts, a high recurrence rate after percutaneous drainage, as well as demonstrate the safety of observing asymptomatic lesions over time. CONCLUSION: We conclude that observation of asymptomatic splenic cysts is safe regardless of size and that aspiration should be reserved for those who are not surgical candidates or in cases of diagnostic uncertainty.

Kinetic analysis of ligand interaction with the gonococcal transferrin-iron acquisition system.

The transferrin iron acquisition system of Neisseria gonorrhoeae consists of two dissimilar transferrin binding proteins (Tbp) A and B. TbpA is a TonB dependent transporter while TbpB is a lipoprotein that makes iron acquisition from transferrin (Tf) more efficient. In an attempt to further define the individual roles of these receptors in the process of Tf-iron acquisition, the kinetics of the receptor proteins in regards to ligand association and dissociation were evaluated. Tf association with TbpB was rapid as compared to TbpA. Tf dissociation from the wild-type receptor occurred in a biphasic manner; an initial rapid release was followed by a slower dissociation over time. Both TbpA and TbpB demonstrated a two-phase release pattern; however, TbpA required both TonB and TbpB for efficient Tf dissociation from the cell surface. The roles of TbpA and TbpB in Tf dissociation were further examined, utilizing previously created HA fusion proteins. Using a Tf-utilization deficient TbpA-HA mutant, we concluded that the slower rate of ligand dissociation demonstrated by the wild-type transporter was a function of successful iron internalization. Insertion into the C-terminus of TbpB decreased the rate of Tf dissociation, while insertion into the N-terminus had no effect on this process. From these studies, we propose that TbpA and TbpB function synergistically during the process of Tf iron acquisition and that TbpB makes the process of Tf-iron acquisition more efficient at least in part by affecting association and dissociation of Tf from the cell surface.

Demonstration and characterization of a specific interaction between gonococcal transferrin binding protein A and TonB.

Iron scavenging by Neisseria gonorrhoeae is accomplished by the expression of receptors that are specific for host iron-binding proteins, such as transferrin and lactoferrin. Efficient transferrin-iron acquisition is dependent on the combined action of two proteins, designated TbpA and TbpB. TbpA is a TonB-dependent outer membrane receptor, whereas TbpB is lipid modified and serves to increase the efficiency of transferrin-iron uptake. Both proteins, together or separately, can be isolated from the gonococcal outer membrane by using affinity chromatography techniques. In the present study, we identified an additional protein in transferrin-affinity preparations, which had an apparent molecular mass of 45 kDa. The ability to copurify this protein by transferrin affinity was dependent upon the presence of TbpA and not TbpB. The amino-terminal sequence of the 45-kDa protein was identical to the amino terminus of gonococcal TonB, indicating that TbpA stably interacted with TonB, without the addition of chemical cross-linkers. Using immunoprecipitation, we could recover TbpA-TonB complexes without the addition of transferrin, suggesting that ligand binding was not a necessary prerequisite for TonB interaction. In contrast, a characterized TonB box mutant of TbpA did not facilitate interaction between these two proteins such that complexes could be isolated. We generated an in-frame deletion of gonococcal TonB, which removed 35 amino acids, including a Neisseria-specific, glycine-rich domain. This mutant protein, like the parental TonB, energized TbpA to enable growth on transferrin. Consistent with the functionality of this deletion derivative, TbpA-TonB complexes could be recovered from this strain. The results of the present study thus begin to define the requirements for a functional interaction between gonococcal TbpA and TonB.